Methods of diagnosis of androgen-dependent prostate cancer, prostate cancer undergoing androgen withdrawal, and androgen-independent prostate cancer

ABSTRACT

Described herein are genes whose expression are up-regulated or down-regulated in prostate cancer. Also described are such genes whose expression is further up-regulated or down-regulated in drug-resistant prostate cancer cells. Related methods and compositions that can be used for diagnosis and treatment of prostate cancer are disclosed. Also described herein are methods that can be used to identify modulators of prostate cancer.

CROSS-REFERENCES TO RELATED APPLICATIONS

This application claims priority from the following applications: U.S.Ser. No. 60/295,917, filed Jun. 4, 2001, U.S. Ser. No. 60/368,689, filedMar. 29, 2002; U.S. Ser. No. 60/350,666, filed Nov. 13, 2001; and U.S.Ser. No. 60/372,246, filed Apr. 12, 2002; each of which is incorporatedherein by reference in its entirety.

FIELD OF THE INVENTION

The invention relates to the identification of nucleic acid and proteinexpression profiles and nucleic acids, products, and antibodies theretothat are involved in prostate cancer; and to the use of such expressionprofiles and compositions in the diagnosis, prognosis, and therapy ofprostate cancer. The invention further relates to methods foridentifying and using agents and/or targets that inhibit prostatecancer.

BACKGROUND OF THE INVENTION

Prostate cancer is the most frequently diagnosed cancer and the secondleading cause of male cancer death in North America and northern Europe.Early detection of prostate cancer using a serum test forprostate-specific antigen (PSA) has dramatically improved the treatmentof the disease (Oesterling (1992) J. Am. Med. Assoc. 267:2236-2238).Treatment of prostate cancer consists largely of surgical prostatectomy,radiation therapy, androgen ablation therapy and chemotherapy. Althoughmany prostate cancer patients are effectively treated, the currenttherapies can all induce serious side effects which diminish quality oflife. Patients who present with metastatic disease are most oftentreated with androgen-ablation therapy. Hormone blockade results insignificant regression of the tumor. However, this treatment rarelycures the patient and invariably results in progression toandrogen-independent disease, which is incurable. Afrin and Stuart(1994) J.S.C. Med. Assoc. 90:231-236.

The identification of novel therapeutic targets and diagnostic markersis essential for improving the current treatment of prostate cancerpatients. Recent advances in molecular medicine have increased theinterest in tumor-specific cell surface antigens that could serve astargets for various immunotherapeutic or small molecule strategies.Antigens suitable for immunotherapeutic strategies should be highlyexpressed in cancer tissues and ideally not expressed in normal adulttissues. Expression in tissues that are dispensable for life, however,may be tolerated. Examples of such antigens include Her2/neu and theB-cell antigen CD20. Humanized monoclonal antibodies directed toHer2/neu (Herceptin) are currently in use for the treatment ofmetastatic breast cancer. Ross and Fletcher (1998) Stem Cells16:413-428. Similarly, anti-CD20 monoclonal antibodies (Rituxin) areused to effectively treat non-Hodgkin's lymphoma. Maloney, et al. (1997)Blood 90:2188-2195; Leget and Czuczman (1998) Curr. Opin. Oncol.10:548-551.

Several potential immunotherapeutic targets have been identified forprostate cancer. They include prostate-specific membrane antigen (PSMA)(Israeli, et al. (1993) Cancer Res. 53:227-230), prostate stem cellantigen (PSCA; Reiter, et al. (1998) Proc. Natl. Acad. Sci. USA95:1735-1740), and serpentine transmembrane epithelial antigen of theprostate (STEAP; Hubert, et al. (1999) Proc. Natl. Acad. Sci. USA96:14529-14534). PSMA is a type II transmembrane hydrolase withsignificant homology to a rat neuropeptidase (Carter, et al. (1996)Proc. Natl. Acad. Sci. USA 93:749-753). Antibodies directed towards PSMAare currently being used to detect metastasized prostate cancer as theProstascint Scan (Sodee, et al. (1996) Clin. Nucl. Med. 21:759-767) andare also being evaluated for treatment of advanced disease (Gregorakis,et al. (1998) Semin. Urol. Oncol. 16:2-12; Liu, et al. (1998) CancerRes. 58:4055-4060; Murphy, et al. (1998) J. Urol. 160:2396-2401). In astudy on bone metastasis of prostate cancer, only 8 out of 18 patientsamples expressed PSMA (Silver, et al. (1997) Clin. Cancer Res.3:81-85). Therefore, it is clear that other targets need to beidentified to manage metastasized disease. PSCA is a member of theThy-1/Ly-6 family of glycosylphosphatidylinositol-linked plasma membraneproteins (Reiter, et al. (1998) Proc. Natl. Acad. Sci. USA95:1735-1740). Immunohistochemical data shows that PSCA is up-regulatedin the majority of prostate cancer epithelia and is also detected inbone metastasis (Gu, et al. (2000) Oncogene 19:1288-1296). Recent workshows that antibodies directed to PSCA can prevent metastatic spread ofprostate cancer in a mouse model (Saffran, et al. (2001) Proc. Natl.Acad. Sci. USA 98:2658-2663). STEAP is a multi-transmembraneprostate-specific protein that may function as a channel or transporterprotein (Hubert, et al. (1999) Proc. Natl. Acad. Sci. USA96:14529-14534). Its protein expression is specific to the basolateralmembranes of normal prostate and prostate cancer epithelia. STEAPexpression was most highly concentrated at cell-cell boundaries,implying a potential function in intercellular communication.Therapeutic monoclonal antibodies have so far not been reported forSTEAP.

SUMMARY OF THE INVENTION

The present invention therefore provides nucleotide sequences of genesthat are up- and down-regulated in androgen-independent prostate cancercells or prostate cells undergoing androgen withdrawal. Such genes areuseful for diagnostic purposes, and also as targets for screening fortherapeutic compounds that modulate prostate cancer, such as hormones orantibodies. Other aspects of the invention will become apparent to theskilled artisan by the following description of the invention.

In one aspect, the present invention provides a method of detecting anandrogen independent prostate cancer-associated transcript in a cellfrom a patient, the method comprising contacting a biological samplefrom the patient with a polynucleotide that selectively hybridizes tonucleic acid molecule comprising a sequence at least 80% identical to asequence as shown in Tables 1A-4.

In one embodiment, the present invention provides a method ofdetermining the level of a prostate cancer associated transcript in acell from a patient.

In one embodiment, the present invention provides a method of detectinga prostate cancer-associated transcript in a cell from a patient, themethod comprising contacting a biological sample from the patient with apolynucleotide that selectively hybridizes to a sequence at least 80%identical to a sequence as shown in Tables 1A-4.

In various embodiments, the polynucleotide selectively hybridizes to asequence at least 95% identical to a sequence as shown in Tables 1A-4;the polynucleotide comprises a sequence as shown in Tables 1A-4; thebiological sample is a tissue sample; the biological sample comprisesisolated nucleic acids, e.g., mRNA; the polynucleotide is labeled, e.g.,with a fluorescent label; the polynucleotide is immobilized on a solidsurface; the patient is undergoing a therapeutic regimen to treatprostate cancer; the patient is suspected of having metastatic prostatecancer; the patient is a human; the patient is suspected of having ataxol-resistant cancer; or the prostate cancer associated transcript ismRNA.

In other embodiments, the method further comprises the step ofamplifying nucleic acids before the step of contacting the biologicalsample with the polynucleotide.

In another aspect, the present invention provides a method of monitoringthe efficacy of a therapeutic treatment of prostate cancer, the methodcomprising the steps of: (i) providing a biological sample from apatient undergoing the therapeutic treatment; and (ii) determining thelevel of a prostate cancer-associated transcript in the biologicalsample by contacting the biological sample with a polynucleotide thatselectively hybridizes to a sequence at least 80% identical to asequence as shown in Tables 1A-4, thereby monitoring the efficacy of thetherapy. In a further embodiment, the patient has metastatic prostatecancer. In a further embodiment, the patient has a drug resistant (e.g.,taxol resistant) form of prostate cancer.

In one embodiment, the method further comprises the step of: (iii)comparing the level of the prostate cancer-associated transcript to alevel of the prostate cancer-associated transcript in a biologicalsample from the patient prior to, or earlier in, the therapeutictreatment.

Additionally, provided herein is a method of evaluating the effect of acandidate prostate cancer drug comprising administering the drug to apatient and removing a cell sample from the patient. The expressionprofile of the cell is then determined. This method may further comprisecomparing the expression profile to an expression profile of a healthyindividual. In a preferred embodiment, said expression profile includesa gene of Tables 1A-4.

In one aspect, the present invention provides an isolated nucleic acidmolecule consisting of a polynucleotide sequence as shown in Tables1A-4.

In one embodiment, an expression vector or cell comprises the isolatednucleic acid.

In one aspect, the present invention provides an isolated polypeptidewhich is encoded by a nucleic acid molecule having polynucleotidesequence as shown in Tables 1A-4.

In another aspect, the present invention provides an antibody thatspecifically binds to an isolated polypeptide which is encoded by anucleic acid molecule having polynucleotide sequence as shown in Tables1A-4.

In certain embodiments, the antibody is conjugated to an effectorcomponent, e.g., a fluorescent label, a radioisotope or a cytotoxicchemical; the antibody is an antibody fragment; or the antibody ishumanized.

In one aspect, the present invention provides a method of detecting aprostate cancer cell in a biological sample from a patient, the methodcomprising contacting the biological sample with an antibody asdescribed herein.

In another aspect, the present invention provides a method of detectingantibodies specific to prostate cancer in a patient, the methodcomprising contacting a biological sample from the patient with apolypeptide encoded by a nucleic acid comprising a sequence from Tables1A-4.

In another aspect, the present invention provides a method foridentifying a compound that modulates a prostate cancer-associatedpolypeptide, the method comprising the steps of: a) contacting thecompound with a prostate cancer-associated polypeptide, the polypeptideencoded by a polynucleotide that selectively hybridizes to a sequence atleast 80% identical to a sequence as shown in Tables 1A-4; and b)determining the functional effect of the compound upon the polypeptide.

In one embodiment, the functional effect is a physical effect, anenzymatic effect, or a chemical effect.

In one embodiment, the polypeptide is expressed in a eukaryotic hostcell or cell membrane. In another embodiment, the polypeptide isrecombinant.

In one embodiment, the functional effect is determined by measuringligand binding to the polypeptide.

In another aspect, the present invention provides a method of inhibitingproliferation of a prostate cancer-associated cell to treat prostatecancer in a patient, the method comprising the step of administering tothe subject a therapeutically effective amount of a compound identifiedas described herein.

In one embodiment, the compound is an antibody.

In another aspect, the present invention provides a drug screening assaycomprising the steps of: a) administering a test compound to a mammalhaving prostate cancer or to a cell sample isolated therefrom; b)comparing the level of gene expression of a polynucleotide thatselectively hybridizes to a sequence at least 80% identical to asequence as shown in Tables 1A-4 in a treated cell or mammal with thelevel of gene expression of the polynucleotide in a control cell sampleor mammal, wherein a test compound that modulates the level ofexpression of the polynucleotide is a candidate for the treatment ofprostate cancer.

In one embodiment, the control is a mammal with prostate cancer or acell sample therefrom that has not been treated with the test compound.In another embodiment, the control is a normal cell or mammal.

In one embodiment, the test compound is administered in varying amountsor concentrations. In another embodiment, the test compound isadministered for varying time periods. In another embodiment, thecomparison can occur after addition or removal of the drug candidate.

In one embodiment, the levels of a plurality of polynucleotides thatselectively hybridize to a sequence at least 80% identical to a sequenceas shown in Tables 1A-4 are individually compared to their respectivelevels in a control cell sample or mammal. In a preferred embodiment theplurality of polynucleotides is from three to ten.

In another aspect, the present invention provides a method for treatinga mammal having prostate cancer comprising administering a compoundidentified by the assay described herein.

In another aspect, the present invention provides a pharmaceuticalcomposition for treating a mammal having prostate cancer, thecomposition comprising a compound identified by the assay describedherein and a physiologically acceptable excipient.

In one aspect, the present invention provides a method of screening drugcandidates by providing a cell expressing a gene that is up- anddown-regulated as in a prostate cancer. In one embodiment, a gene isselected from Tables 1A-4. The method further includes adding a drugcandidate to the cell and determining the effect of the drug candidateon the expression of the expression profile gene.

In one embodiment, the method of screening drug candidates includescomparing the level of expression in the absence of the drug candidateto the level of expression in the presence of the drug candidate,wherein the concentration of the drug candidate can vary when present,and wherein the comparison can occur after addition or removal of thedrug candidate. In a preferred embodiment, the cell expresses at leasttwo expression profile genes. The profile genes may show an increase ordecrease.

Also provided is a method of evaluating the effect of a candidateprostate cancer drug comprising administering the drug to a transgenicanimal expressing or over-expressing the prostate cancer modulatoryprotein, or an animal lacking the prostate cancer modulatory protein,for example as a result of a gene knockout.

Moreover, provided herein is a biochip comprising one or more nucleicacid segments of Tables 1A-4, wherein the biochip comprises fewer than1000 nucleic acid probes. Preferably, at least two nucleic acid segmentsare included. More preferably, at least three nucleic acid segments areincluded.

Furthermore, a method of diagnosing a disorder associated with prostatecancer is provided. The method comprises determining the expression of agene of Tables 1A-4, in a first tissue type of a first individual, andcomparing the distribution to the expression of the gene from a secondnormal tissue type from the first individual or a second unaffectedindividual. A difference in the expression indicates that the firstindividual has a disorder associated with prostate cancer.

In a further embodiment, the biochip also includes a polynucleotidesequence of a gene that is not up- and down-regulated in prostatecancer.

In one embodiment a method for screening for a bioactive agent capableof interfering with the binding of a prostate cancer modulating protein(prostate cancer modulatory protein) or a fragment thereof and anantibody which binds to said prostate cancer modulatory protein orfragment thereof. In a preferred embodiment, the method comprisescombining a prostate cancer modulatory protein or fragment thereof, acandidate bioactive agent and an antibody which binds to said prostatecancer modulatory protein or fragment thereof. The method furtherincludes determining the binding of said prostate cancer modulatoryprotein or fragment thereof and said antibody. Wherein there is a changein binding, an agent is identified as an interfering agent. Theinterfering agent can be an agonist or an antagonist. Preferably, theagent inhibits prostate cancer.

Also provided herein are methods of eliciting an immune response in anindividual. In one embodiment a method provided herein comprisesadministering to an individual a composition comprising a prostatecancer modulating protein, or a fragment thereof. In another embodiment,the protein is encoded by a nucleic acid selected from those of Tables1A-4.

Further provided herein are compositions capable of eliciting an immuneresponse in an individual. In one embodiment, a composition providedherein comprises a prostate cancer modulating protein, preferablyencoded by a nucleic acid of Tables 1A-4, or a fragment thereof, and apharmaceutically acceptable carrier. In another embodiment, saidcomposition comprises a nucleic acid comprising a sequence encoding aprostate cancer modulating protein, preferably selected from the nucleicacids of Tables 1A-4 and a pharmaceutically acceptable carrier.

Also provided are methods of neutralizing the effect of a prostatecancer protein, or a fragment thereof, comprising contacting an agentspecific for said protein with said protein in an amount sufficient toeffect neutralization. In another embodiment, the protein is encoded bya nucleic acid selected from those of Tables 1A-4. In another aspect ofthe invention, a method of treating an individual for prostate cancer isprovided. In one embodiment, the method comprises administering to saidindividual an inhibitor of a prostate cancer modulating protein. Inanother embodiment, the method comprises administering to a patienthaving prostate cancer an antibody to a prostate cancer modulatingprotein conjugated to a therapeutic moiety. Such a therapeutic moietycan be a cytotoxic agent or a radioisotope.

DETAILED DESCRIPTION OF THE INVENTION

In accordance with the objects outlined above, the present inventionprovides novel methods for diagnosis and evaluation ofandrogen-dependent prostate cells (malignant or non-malignant), prostatecells undergoing androgen withdrawal, and androgen-independent prostatecancer, as well as methods for treating androgen-dependent prostatecells (malignant or non-malignant), prostate cancer undergoing androgenwithdrawal, and androgen-independent prostate cancer. The currentSpecification incorporates the text of U.S. Ser. No. 09/976,858, filedOct. 12, 2001, U.S. Ser. No. 60/295,917, filed Jun. 4, 2001, U.S. Ser.No. 60/368,689, filed Mar. 29, 2002; U.S. Ser. No. 60/350,666, filedNov. 13, 2001; and U.S. Ser. No. 60/372,246, filed Apr. 12, 2002.

Table 1A provides unigene cluster identification numbers for thenucleotide sequence of genes that exhibit increased or decreasedexpression in androgen-independent prostate cancer samples. Table 1Aalso provides an exemplar accession number that provides a nucleotidesequence that is part of the unigene cluster. The expression patterns ofthe genes of Table 1A can be broadly defined into the followingcategories: Genes that are expressed early in the time course, then dropoff in expression, and then express again with emergence ofandrogen-independence (hi-lo-hi pattern in table 1A). Genes that areexpressed early in the time course, then drop off in expression, and donot express again with emergence of androgen-independence (hi-lo-lopattern in 1A). Genes that are not expressed early in the time course,but express only with emergence of androgen-independence (lo-lo-hipattern in table 1A). Genes that are not expressed early in the timecourse, but then express as androgen is withdrawn and continue toexpress with emergence of androgen-independence (lo-hi-hi pattern intable 1A). Genes that are not expressed early in the time course, butthen express as androgen is withdrawn and drop, off again with emergenceof androgen-independence (lo-hi-lo pattern in table 1A).

Tables 2A-C provide unigene cluster identification numbers for thenucleotide sequence of genes that exhibit increased or decreasedexpression in androgen-dependent prostate cancer, prostate cancerundergoing androgen withdrawal and androgen-independent prostate cancer.Tables 2A-C also provide an exemplar accession number that provides anucleotide sequence that is part of the unigene cluster. The expressionpatterns of the genes of Tables 2A-C can be broadly defined into thefollowing 6 categories:

Genes that are expressed early in the time course of androgenwithdrawal, then drop off in expression, and then express again withemergence of androgen-independence (hi-lo-lo-hi pattern in Table 2A).Genes that are expressed early in the time course, then drop off inexpression immediately after androgen-withdrawal, and do not expressagain with emergence of androgen-independence (hi-lo-lo-lo pattern inTable 2A). Genes that are expressed early in the time course, then dropoff in expression after several days of androgen withdrawal, and do notexpress again with emergence of androgen-independence (hi-hi-lo-lopattern in Table 2A). Genes that are not expressed early in the timecourse, but express only with emergence of androgen-independence(lo-lo-lo-hi pattern in Table 2A). Genes that are not expressed early inthe time course, but then express as androgen is withdrawn and continueto express with emergence of androgen-independence (lo-lo-hi-hi patternin Table 2A). Genes that are not expressed early in the time course, butthen express as androgen is withdrawn and drop off again with emergenceof androgen-independence (lo-lo-hi-lo pattern in Table 2A).

Definitions

The term “androgen ablation therapy” refers to techniques for theremoval or destruction of sources of male hormones, such astestosterone. These techniques include, for example, 1) surgical removalof the testicles, 2) medications such as gonadatropin releasing hormoneanalogs that inhibit testosterone production, or 3) anti-androgenicdrugs that block androgen receptors.

The term “androgen-independent prostate cancer protein” or“androgen-independent prostate cancer polynucleotide” or“androgen-independent prostate cancer-associated transcript” refers tonucleic acid and polypeptide polymorphic variants, alleles, mutants, andinterspecies homologues that: (1) have a nucleotide sequence that hasgreater than about 60% nucleotide sequence identity, 65%, 70%, 75%, 80%,85%, 90%, preferably 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% orgreater nucleotide sequence identity, preferably over a region of over aregion of at least about 25, 50, 100, 200, 500, 1000, or morenucleotides, to a nucleotide sequence of or associated with a unigenecluster of Tables 1A-4; (2) bind to antibodies, e.g., polyclonalantibodies, raised against an immunogen comprising an amino acidsequence encoded by a nucleotide sequence of or associated with aunigene cluster of Tables 1A-4 and conservatively modified variantsthereof; (3) specifically hybridize under stringent hybridizationconditions to a nucleic acid sequence, or the complement thereof ofTables 1A-4 and conservatively modified variants thereof; or (4) have anamino acid sequence that has greater than about 60% amino acid sequenceidentity, 65%, 70%, 75%, 80%, 85%, 90%, preferably 91%, 92%, 93%, 94%,95%, 96%, 97%, 98% or 99% or greater amino sequence identity, preferablyover a region of over a region of at least about 25, 50, 100, 200, 500,1000, or more amino acid, to an amino acid sequence encoded by anucleotide sequence of or associated with a unigene cluster of Tables1A-4. These polynucleotides or proteins may also be expressed during aperiod following androgen withdrawal. A polynucleotide or polypeptidesequence is typically from a mammal including, but not limited to,primate, e.g., human; rodent, e.g., rat, mouse, hamster; cow, pig,horse, sheep, or other mammal. A “prostate cancer polypeptide” and a“prostate cancer polynucleotide,” include both naturally occurring orrecombinant forms, and may refer to those polypeptides orpolynucleotides which are expressed in prostate proliferative cells.

A “full length” prostate cancer protein or nucleic acid refers to aprostate cancer polypeptide or polynucleotide sequence, or a variantthereof, that contains the elements normally contained in one or morenaturally occurring, wild type prostate cancer polynucleotide orpolypeptide sequences. The “full length” may be prior to, or after,various stages of post-translation processing or splicing, includingalternative splicing.

“Biological sample” as used herein is a sample of biological tissue orfluid that contains nucleic acids or polypeptides, e.g., of a prostatecancer protein, polynucleotide or transcript. Such samples include, butare not limited to, tissue isolated from primates, e.g., humans, orrodents, e.g., mice, and rats. Biological samples may also includesections of tissues such as biopsy and autopsy samples, frozen sectionstaken for histology purposes, blood, plasma, serum, sputum, stool,tears, mucus, hair, skin, etc. Biological samples also include explantsand primary and/or transformed cell cultures derived from patienttissues. A biological sample is typically obtained from a eukaryoticorganism, most preferably a mammal such as a primate e.g., chimpanzee orhuman; cow; dog; cat; a rodent, e.g., guinea pig, rat, mouse; rabbit; ora bird; reptile; or fish.

“Providing a biological sample” means to obtain a biological sample foruse in methods described in this invention. Most often, this will bedone by removing a sample of cells from an animal, but can also beaccomplished by using previously isolated cells (e.g., isolated byanother person, at another time, and/or for another purpose), bycollecting a sample which contains a soluble polypeptide or nucleic acidderived from a prostate cell, or by performing the methods of theinvention in vivo. Archival tissues, having treatment or outcomehistory, will be particularly useful.

The terms “identical” or percent “identity,” in the context of two ormore nucleic acids or polypeptide sequences, refer to two or moresequences or subsequences that are the same or have a specifiedpercentage of amino acid residues or nucleotides that are the same(i.e., about 60% identity, preferably 70%, 75%, 80%, 85%, 90%, 91%, 92%,93%, 94%, 95%, 96%, 97%, 98%, 99%, or higher identity over a specifiedregion, when compared and aligned for maximum correspondence over acomparison window or designated region) as measured using a BLAST orBLAST 2.0 sequence comparison algorithms with default parametersdescribed below, or by manual alignment and visual inspection (see,e.g., NCBI web site http://www.ncbi.nlm.nih.gov/BLAST/ or the like).Such sequences are then said to be “substantially identical.” Thisdefinition also refers to, or may be applied to, the compliment of atest sequence. The definition also includes sequences that havedeletions and/or additions, as well as those that have substitutions, aswell as naturally occurring, e.g., polymorphic or allelic variants, andman-made variants. As described below, the preferred algorithms canaccount for gaps and the like. Preferably, identity exists over a regionthat is at least about 25 amino acids or nucleotides in length, or morepreferably over a region that is 50-100 amino acids or nucleotides inlength.

For sequence comparison, typically one sequence acts as a referencesequence, to which test sequences are compared. When using a sequencecomparison algorithm, test and reference sequences are entered into acomputer, subsequence coordinates are designated, if necessary, andsequence algorithm program parameters are designated. Preferably,default program parameters can be used, or alternative parameters can bedesignated. The sequence comparison algorithm then calculates thepercent sequence identities for the test sequences relative to thereference sequence, based on the program parameters.

A “comparison window”, as used herein, includes reference to a segmentof one of the number of contiguous positions selected from the groupconsisting typically of from 20 to 600, usually about 50 to about 200,more usually about 100 to about 150 in which a sequence may be comparedto a reference sequence of the same number of contiguous positions afterthe two sequences are optimally aligned. Methods of alignment ofsequences for comparison are well-known in the art. Optimal alignment ofsequences for comparison can be conducted, e.g., by the local homologyalgorithm of Smith and Watermnan (1981) Appl. Math. 2:482, by thehomology alignment algorithm of Needleman and Wunsch (1970) J. Mol.Biol. 48:443-453, by the search for similarity method of Pearson andLipman (1988) Proc. Nat'l. Acad. Sci. USA 85:2444-2448, by computerizedimplementations of these algorithms (GAP, BESTFIT, FASTA, and TFASTA inthe Wisconsin Genetics Software Package, Genetics Computer Group, 575Science Dr., Madison, Wis.), or by manual alignment and visualinspection (see, e.g., Ausubel, et al. (eds. 1995 and supplements)Current Protocols in Molecular Biology Lippincott).

Preferred examples of algorithms that are suitable for determiningpercent sequence identity and sequence similarity include the BLAST andBLAST 2.0 algorithms, which are a described in Altschul, et al. (1977)Nuc. Acids Res. 25:3389-3402 and Altschul, et al. (1990) J. Mol. Biol.215:403-410. BLAST and BLAST 2.0 are used, with the parameters describedherein, to determine percent sequence identity for the nucleic acids andproteins of the invention. Software for performing BLAST analyses ispublicly available through the National Center for BiotechnologyInformation (http://www.ncbi.nlm.nih.gov/). This algorithm involvesfirst identifying high scoring sequence pairs (HSPs) by identifyingshort words of length W in the query sequence, which either match orsatisfy some positive-valued threshold score T when aligned with a wordof the same length in a database sequence. T is referred to as theneighborhood word score threshold (Altschul, et al., supra). Theseinitial neighborhood word hits act as seeds for initiating searches tofind longer HSPs containing them. The word hits are extended in bothdirections along each sequence for as far as the cumulative alignmentscore can be increased. Cumulative scores are calculated using, e.g.,for nucleotide sequences, the parameters M (reward score for a pair ofmatching residues; always >0) and N (penalty score for mismatchingresidues; always <0). For amino acid sequences, a scoring matrix is usedto calculate the cumulative-score. Extension of the word hits in eachdirection are halted when: the cumulative alignment score falls off bythe quantity X from its maximum achieved value; the cumulative scoregoes to zero or below, due to the accumulation of one or morenegative-scoring residue alignments; or the end of either sequence isreached. The BLAST algorithm parameters W, T, and X determine thesensitivity and speed of the alignment. The BLASTN program (fornucleotide sequences) uses as defaults a wordlength (W) of 11, anexpectation (E) of 10, M=5, N=−4 and a comparison of both strands. Foramino acid sequences, the BLASTP program uses as defaults a wordlengthof 3, and expectation (E) of 10, and the BLOSUM62 scoring matrix (seeHenikoff and Henikoff (1989) Proc. Natl. Acad. Sci. USA 89:10915-919)alignments (B) of 50, expectation (E) of 10, M=5, N=−4, and a comparisonof both strands.

The BLAST algorithm also performs a statistical analysis of thesimilarity between two sequences (see, e.g., Karlin and Altschul (1993)Proc. Nat'l. Acad. Sci. USA 90:5873-5787). One measure of similarityprovided by the BLAST algorithm is the smallest sum probability (P(N)),which provides an indication of the probability by which a match betweentwo nucleotide or amino acid sequences would occur by chance. Forexample, a nucleic acid is considered similar to a reference sequence ifthe smallest sum probability in a comparison of the test nucleic acid tothe reference nucleic acid is less than about 0.2, more preferably lessthan about 0.01, and most preferably less than about 0.001. Log valuesmay be large negative numbers, e.g., 5, 10, 20, 30, 40, 40, 70, 90, 110,150, 170, etc.

An indication that two nucleic acid sequences or polypeptides aresubstantially identical is that the polypeptide encoded by the firstnucleic acid is immunologically cross reactive with the antibodiesraised against the polypeptide encoded by the second nucleic acid, asdescribed below. Thus, a polypeptide is typically substantiallyidentical to a second polypeptide, e.g., where the two peptides differonly by conservative substitutions. Another indication that two nucleicacid sequences are substantially identical is that the two molecules ortheir complements hybridize to each other under stringent conditions, asdescribed below. Yet another indication that two nucleic acid sequencesare substantially identical is that the same primers can be used toamplify the sequences.

A “host cell” is a naturally occurring cell or a transformed cell thatcontains an expression vector and supports the replication or expressionof the expression vector. Host cells may be cultured cells, explants,cells in vivo, and the like. Host cells may be prokaryotic cells such asE. coli, or eukaryotic cells such as yeast, insect, amphibian, ormammalian cells such as CHO, HeLa, and the like (see, e.g., the AmericanType Culture Collection catalog or web site, www.atcc.org).

The terms “isolated,” “purified,” or “biologically pure” refer tomaterial that is substantially or essentially free from components thatnormally accompany it as found in its native state. Purity andhomogeneity are typically determined using analytical chemistrytechniques such as polyacrylamide gel electrophoresis or highperformance liquid chromatography. A protein or nucleic acid that is thepredominant species present in a preparation is substantially purified.In particular, an isolated nucleic acid is separated from some openreading frames that naturally flank the gene and encode proteins otherthan protein encoded by the gene. The term “purified” in someembodiments denotes that a nucleic acid or protein gives rise toessentially one band in an electrophoretic gel. Preferably, it meansthat the nucleic acid or protein is at least 85% pure, more preferablyat least 95% pure, and most preferably at least 99% pure. “Purify” or“purification” in other embodiments means removing at least onecontaminant from the composition to be purified. In this sense,purification does not require that the purified compound be homogenous,e.g., 100% pure.

The terms “polypeptide,” “peptide,” and “protein” are usedinterchangeably herein to refer to a polymer of amino acid residues. Theterms apply to amino acid polymers in which one or more amino acidresidue is an artificial chemical mimetic of a corresponding naturallyoccurring amino acid, as well as to naturally occurring amino acidpolymers, those containing modified residues, and non-naturallyoccurring amino acid polymer. Certain diagnostic methods may evaluatesecreted or breakdown products present only because the producing cellis present, and would otherwise be absent in a normal individual.

The term “amino acid” refers to naturally occurring and synthetic aminoacids, as well as amino acid analogs and amino acid mimetics thatfunction similarly to the naturally occurring amino acids. Naturallyoccurring amino acids are those encoded by the genetic code, as well asthose amino acids that are later modified, e.g., hydroxyproline,γ-carboxyglutamate, and O-phosphoserine. Amino acid analogs refers tocompounds that have the same basic chemical structure as a naturallyoccurring amino acid, e.g., an a carbon that is bound to a hydrogen, acarboxyl group, an amino group, and an R group, e.g., homoserine,norleucine, methionine sulfoxide, methionine methyl sulfonium. Suchanalogs may have modified R groups (e.g., norleucine) or modifiedpeptide backbones, but retain the same basic chemical structure as anaturally occurring amino acid. Amino acid mimetics refers to chemicalcompounds that have a structure that is different from the generalchemical structure of an amino acid, but that functions similarly to anaturally occurring amino acid.

Amino acids may be referred to herein by either their commonly knownthree letter symbols or by the one-letter symbols recommended by theIUPAC-IUB Biochemical Nomenclature Commission. Nucleotides, likewise,may be referred to by their commonly accepted single-letter codes.

“Conservatively modified variants” applies to both amino acid andnucleic acid sequences. With respect to particular nucleic acidsequences, conservatively modified variants refers to those nucleicacids which encode identical or essentially identical amino acidsequences, or where the nucleic acid does not encode an amino acidsequence, to essentially identical or associated, e.g., naturallycontiguous, sequences. Because of the degeneracy of the genetic code, alarge number of functionally identical nucleic acids encode mostproteins. For instance, the codons GCA, GCC, GCG, and GCU encode theamino acid alanine. Thus, at every position where an alanine isspecified by a codon, the codon can be altered to another of thecorresponding codons described without altering the encoded polypeptide.Such nucleic acid variations are “silent variations,” which are onespecies of conservatively modified variations. Every nucleic acidsequence herein which encodes a polypeptide also describes silentvariations of the nucleic acid. One of skill will recognize that incertain contexts each codon in a nucleic acid (except AUG, which isordinarily the only codon for methionine, and TGG, which is ordinarilythe only codon for tryptophan) can be modified to yield a functionallyidentical molecule. Accordingly, often silent variations of a nucleicacid which encodes a polypeptide is implicit in a described sequencewith respect to the expression product, but not with respect to actualprobe sequences.

As to amino acid sequences, one of skill will recognize that individualsubstitutions, deletions or additions to a nucleic acid, peptide,polypeptide, or protein sequence which alters, adds or deletes a singleamino acid or a small percentage of amino acids in the encoded sequenceis a “conservatively modified variant” where the alteration results inthe substitution of an amino acid with a chemically similar amino acid.Conservative substitutions providing functionally similar amino acidsare well known in the art. Such conservatively modified variants are inaddition to and do not exclude polymorphic variants, interspecieshomologs, and alleles of the invention, typically conservativesubstitutions for one another: 1) Alanine (A), Glycine (G); 2) Asparticacid (D), Glutamic acid (E); 3) Asparagine (N), Glutamine (Q); 4)Arginine (R), Lysine (K); 5) Isoleucine (I), Leucine (L), Methionine(M), Valine (V); 6) Phenylalanine (F), Tyrosine (Y), Tryptophan (W); 7)Serine (S), Threonine (T); and 8) Cysteine (C), Methionine (M) (see,e.g., Creighton (1984) Proteins Freeman).

Macromolecular structures such as polypeptide structures can bedescribed in terms of various levels of organization. For a generaldiscussion of this organization, see, e.g., Alberts, et al. (2001)Molecular Biology of the Cell (4th ed.) and Cantor and Schimmel (1980)Biophysical Chemistry Part I: The Conformation of BiologicalMacromolecules Freeman. “Primary structure” refers to the amino acidsequence of a particular peptide. “Secondary structure” refers tolocally ordered, three dimensional structures within a polypeptide.These structures are commonly known as domains. Domains are portions ofa polypeptide that often form a compact unit of the polypeptide and aretypically 25 to approximately 500 amino acids long. Typical domains aremade up of sections of lesser organization such as stretches of β-sheetand α-helices. “Tertiary structure” refers to the complete threedimensional structure of a polypeptide monomer. “Quaternary structure”refers to the three dimensional structure formed, usually by thenoncovalent association of independent tertiary units. Anisotropic termsare also known as energy terms.

“Nucleic acid” or “oligonucleotide” or “polynucleotide” or grammaticalequivalents used herein means at least two nucleotides covalently linkedtogether. Oligonucleotides are typically from about 5, 6, 7, 8, 9, 10,12, 15, 25, 30, 40, 50 or more nucleotides in length, up to about 100nucleotides in length. Nucleic acids and polynucleotides are a polymersof virtually any length, including longer lengths, e.g., 200, 300, 500,1000, 2000, 3000, 5000, 7000, 10,000, etc. A nucleic acid of the presentinvention will generally contain phosphodiester bonds, although in somecases, nucleic acid analogs are included that may have alternatebackbones, comprising, e.g., phosphoramidate, phosphorothioate,phosphorodithioate, or O-methylphosphoroamidite linkages (see Eckstein(1992) Oligonucleotides and Analogues: A Practical Approach, OxfordUniversity Press); and peptide nucleic acid backbones and linkages.Other analog nucleic acids include those with positive backbones;non-ionic backbones, and non-ribose backbones, including those describedin U.S. Pat. Nos. 5,235,033 and 5,034,506, and Chapters 6 and 7, ASCSymposium Series 580, Sanghvi and Cook (eds. 1994) CarbohydrateModifications in Antisense Research ACS Symposium Series 580. Nucleicacids containing one or more carbocyclic sugars are also included withinone definition of nucleic acids. Modifications of the ribose-phosphatebackbone may be done for a variety of reasons, e.g., to increase thestability and half-life of such molecules in physiological environmentsor as probes on a biochip. Mixtures of naturally occurring nucleic acidsand analogs can be made; alternatively, mixtures of different nucleicacid analogs, and mixtures of naturally occurring nucleic acids andanalogs may be made.

A variety of references disclose such nucleic acid analogs, including,for example, phosphoramidate (Beaucage, et al. (1993) Tetrahedron49(10):1925-1963 and references therein; Letsinger (1970) J. Org. Chem.35:3800-3803; Sprinzl, et al. (1977) Eur. J. Biochem. 81:579-589;Letsinger, et al. (1986) Nucl. Acids Res. 14:3487-499; Sawai, et al(1984) Chem. Lett. 805, Letsinger, et al. (1988) J. Am. Chem. Soc.110:4470-4471; and Pauwels, et al. (1986) Chemica Scripta 26:141-149),phosphorothioate (Mag, et al. (1991) Nucleic Acids Res. 19:1437-441; andU.S. Pat. No. 5,644,048), phosphorodithioate (Briu, et al. (1989). Am.Chem. Soc. 111:2321-xxx, O-methylphosphoroamidite linkages (see Eckstein(1992) Oligonucleotides and Analogues: A Practical Approach OxfordUniversity Press), and peptide nucleic acid backbones and linkages (seeEgholm (1992) J. Am. Chem. Soc. 114:1895-1897; Meier, et al. (1992)Chem. Int. Ed. Engl. 31:1008-1010; Nielsen (1993) Nature 365:566-568;Carlsson, et al. (1996) Nature 380:207, each of which is incorporated byreference). Other analog nucleic acids include those with positivebackbones (Denpcy, et al. (1995) Proc. Natl. Acad. Sci. USA 92:6097-101;non-ionic backbones (U.S. Pat. Nos. 5,386,023, 5,637,684, 5,602,240,5,216,141 and 4,469,863; Kiedrowshi, et al. (1991) Angew. Chem. Intl.Ed. English 30:423-426; Letsinger, et al. (1988) J. Am. Chem. Soc.110:4470; Letsinger, et al. (1994) Nucleoside and Nucleotide13:1597-xxx; Chapters 2 and 3 in Sanghvi and Cook (eds. 1994)Carbohydrate Modifications in Antisense Research ACS Symposium Series580; Mesmaeker, et al. (1994) Bioorganic and Medicinal Chem. Lett.4:395-xxx; Jeffs, et al. (1994) J. Biomolecular NMR 34:17; Horn (1996)Tetrahedron Lett. 37:743-xxx) and non-ribose backbones, including thosedescribed in U.S. Pat. Nos. 5,235,033 and 5,034,506, and Chapters 6 and7 in Sanghvi and Cook (eds. 1994) Carbohydrate Modifications inAntisense Research ACS Symposium Series 580. Nucleic acids containingone or more carbocyclic sugars are also included within one definitionof nucleic acids (see Jenkins, et al. (1995) Chem. Soc. Rev.xx:169-176). Several nucleic acid analogs are described in Rawls (p. 35,Jun. 2, 1997) C&E News. Each of these references is hereby expresslyincorporated by reference.

Particularly preferred are peptide nucleic acids (PNA) which includespeptide nucleic acid analogs. These backbones are substantiallynon-ionic under neutral conditions, in contrast to the highly chargedphosphodiester backbone of naturally occurring nucleic acids. Thisresults in two advantages. First, the PNA backbone exhibits improvedhybridization kinetics. PNAs have larger changes in the meltingtemperature (T_(m)) for mismatched versus perfectly matched base pairs.DNA and RNA typically exhibit a 2-4° C. drop in T_(m) for an internalmismatch. With the non-ionic PNA backbone, the drop is closer to 7-9° C.Similarly, due to their non-ionic nature, hybridization of the basesattached to these backbones is relatively insensitive to saltconcentration. In addition, PNAs are not degraded by cellular enzymes,and thus can be more stable.

The nucleic acids may be single stranded or double stranded, asspecified, or contain portions of both double stranded or singlestranded sequence. As will be appreciated by those in the art, thedepiction of a single strand also defines the sequence of thecomplementary strand; thus the sequences described herein also providethe complement of the sequence. The nucleic acid may be DNA, bothgenomic and cDNA, RNA or a hybrid, where the nucleic acid may containcombinations of deoxyribo- and ribo-nucleotides, and combinations ofbases, including uracil, adenine, thymine, cytosine, guanine, inosine,xanthine hypoxanthine, isocytosine, isoguanine, etc. “Transcript”typically refers to a naturally occurring RNA, e.g., a pre-mRNA, hnRNA,or mRNA. As used herein, the term “nucleoside” includes nucleotides andnucleoside and nucleotide analogs, and modified nucleosides such asamino modified nucleosides. In addition, “nucleoside” includesnon-naturally occurring analog structures. Thus, e.g., the individualunits of a peptide nucleic acid, each containing a base, are referred toherein as a nucleoside.

A “label” or a “detectable moiety” is a composition detectable byspectroscopic, photochemical, biochemical, immunochemical, chemical, orother physical means. For example, useful labels include ³²P,fluorescent dyes, electron-dense reagents, enzymes (e.g., as commonlyused in an ELISA), biotin, digoxigenin, or haptens and proteins or otherentities which can be made detectable, e.g., by incorporating aradiolabel into the peptide or used to detect antibodies specificallyreactive with the peptide. The labels may be incorporated into theprostate cancer nucleic acids, proteins, and antibodies at virtually anyposition. Many methods for conjugating the antibody to the label may beemployed, including those methods described by Hunter, et al. (1962)Nature, 144:945; David, et al. (1974) Biochemistry 13:1014-1021; Pain,et al. (1981) J. Immunol. Meth. 40:219-230; and Nygren (1982) J.Histochem. and Cytochem. 30:407-412.

An “effector” or “effector moiety” or “effector component” is a moleculethat is bound (or linked, or conjugated), either covalently, through alinker or a chemical bond, or noncovalently, through ionic, van derWaals, electrostatic, or hydrogen bonds, to an antibody. The “effector”can be a variety of molecules including, e.g., detection moietiesincluding radioactive compounds, fluorescent compounds, an enzyme orsubstrate, tags such as epitope tags, a toxin; activatable moieties, achemotherapeutic agent; a lipase; an antibiotic; or a radioisotopeemitting “hard” e.g., beta radiation.

A “labeled nucleic acid probe or oligonucleotide” is one that is bound,either covalently, through a linker or a chemical bond, ornoncovalently, through ionic, van der Waals, electrostatic, or hydrogenbonds to a label such that the presence of the probe may be detected bydetecting the presence of the label bound to the probe. Alternatively,method using high affinity interactions may achieve the same resultswhere one of a pair of binding partners binds to the other, e.g.,biotin, streptavidin.

As used herein a “nucleic acid probe or oligonucleotide” is defined as anucleic acid capable of binding to a target nucleic acid ofcomplementary sequence through one or more types of chemical bonds,usually through complementary base pairing, usually through hydrogenbond formation. As used herein, a probe may include natural (i.e., A, G,C, or T) or modified bases (7-deazaguanosine, inosine, etc.). Inaddition, the bases in a probe may be joined by a linkage other than aphosphodiester bond, so long as it does not functionally interfere withhybridization. Thus, e.g., probes may be peptide nucleic acids in whichthe constituent bases are joined by peptide bonds rather thanphosphodiester linkages. It will be understood by one of skill in theart that probes may bind target sequences lacking completecomplementarity with the probe sequence depending upon the stringency ofthe hybridization conditions. The probes are preferably directly labeledas with isotopes, chromophores, lumiphores, chromogens, or indirectlylabeled such as with biotin to which a streptavidin complex may laterbind. By assaying for the presence or absence of the probe, one candetect the presence or absence of the select sequence or subsequence.Diagnosis or prognosis may be based at the genomic level, or at thelevel of RNA or protein expression.

The term “recombinant” when used with reference, e.g., to a cell, ornucleic acid, protein, or vector, indicates that the cell, nucleic acid,protein or vector, has been modified by the introduction of aheterologous nucleic acid or protein or the alteration of a nativenucleic acid or protein, or that the cell is derived from a cell somodified. Thus, e.g., recombinant cells express genes that are not foundwithin the native (non-recombinant) form of the cell or express nativegenes that are otherwise abnormally expressed, under expressed or notexpressed at all. By the term “recombinant nucleic acid” herein is meantnucleic acid, originally formed in vitro, in general, by themanipulation of nucleic acid, e.g., using polymerases and endonucleases,in a form not normally found in nature. In this manner, operably linkageof different sequences is achieved. Thus an isolated nucleic acid, in alinear form, or an expression vector formed in vitro by ligating DNAmolecules that are not normally joined, are both considered recombinantfor the purposes of this invention. It is understood that once arecombinant nucleic acid is made and reintroduced into a host cell ororganism, it will replicate non-recombinantly, i.e., using the in vivocellular machinery of the host cell rather than in vitro manipulations;however, such nucleic acids, once produced recombinantly, althoughsubsequently replicated non-recombinantly, are still consideredrecombinant for the purposes of the invention. Similarly, a “recombinantprotein” is a protein made using recombinant techniques, i.e., throughthe expression of a recombinant nucleic acid as depicted above.

The term “heterologous” when used with reference to portions of anucleic acid indicates that the nucleic acid comprises two or moresubsequences that are not normally found in the same relationship toeach other in nature. For instance, the nucleic acid is typicallyrecombinantly produced, having two or more sequences, e.g., fromunrelated genes arranged to make a new functional nucleic acid, e.g., apromoter from one source and a coding region from another source.Similarly, a heterologous protein will often refer to two or moresubsequences that are not found in the same relationship to each otherin nature (e.g., a fusion protein).

A “promoter” is defined as an array of nucleic acid control sequencesthat direct transcription of a nucleic acid. As used herein, a promoterincludes necessary nucleic acid sequences near the start site oftranscription, such as, in the case of a polymerase II type promoter, aTATA element. A promoter also optionally includes distal enhancer orrepressor elements, which can be located as much as several thousandbase pairs from the start site of transcription. A “constitutive”promoter is a promoter that is active under most environmental anddevelopmental conditions. An “inducible” promoter is a promoter that isactive under environmental or developmental regulation. The term“operably linked” refers to a functional linkage between a nucleic acidexpression control sequence (such as a promoter, or array oftranscription factor binding sites) and a second nucleic acid sequence,wherein the expression control sequence directs transcription of thenucleic acid corresponding to the second sequence.

An “expression vector” is a nucleic acid construct, generatedrecombinantly or synthetically, with a series of specified nucleic acidelements that permit transcription of a particular nucleic acid in ahost cell. The expression vector can be part of a plasmid, virus, ornucleic acid fragment. Typically, the expression vector includes anucleic acid to be transcribed operably linked to a promoter.

The phrase “selectively (or specifically) hybridizes to” refers to thebinding, duplexing, or hybridizing of a molecule only to a particularnucleotide sequence under stringent hybridization conditions when thatsequence is present in a complex mixture (e.g., total cellular orlibrary DNA or RNA).

The phrase “stringent hybridization conditions” refers to conditionsunder which a probe will hybridize to its target subsequence, typicallyin a complex mixture of nucleic acids, but to no other sequences.Stringent conditions are sequence-dependent and will be different indifferent circumstances. Longer sequences hybridize specifically athigher temperatures. An extensive guide to the hybridization of nucleicacids is found “Overview of principles of hybridization and the strategyof nucleic acid assays” in Tijssen (1993) Hybridization with NucleicProbes (Techniques in Biochemistry and Molecular Biology vol. 24)Elsevier. Generally, stringent conditions are selected to be about 5-10°C. lower than the thermal melting point (T_(m)) for the specificsequence at a defined ionic strength pH. The T_(m) is the temperature(under defined ionic strength, pH, and nucleic concentration) at which50% of the probes complementary to the target hybridize to the targetsequence at equilibrium (as the target sequences are present in excess,at T_(m), 50% of the probes are occupied at equilibrium). Stringentconditions will be those in which the salt concentration is less thanabout 1.0 M sodium ion, typically about 0.01 to 1.0 M sodium ionconcentration (or other salts) at pH 7.0 to 8.3 and the temperature isat least about 30° C. for short probes (e.g., 10 to 50 nucleotides) andat least about 60° C. for long probes (e.g., greater than 50nucleotides). Stringent conditions may also be achieved with theaddition of destabilizing agents such as formamide. For selective orspecific hybridization, a positive signal is at least two timesbackground, preferably 10 times background hybridization. Exemplarystringent hybridization conditions can be as following: 50% formamide,5×SSC, and 1% SDS, incubating at 42° C., or, 5×SSC, 1% SDS, incubatingat 65° C., with wash in 0.2×SSC, and 0.1% SDS at 65° C. For PCR, atemperature of about 36° C. is typical for low stringency amplification,although annealing temperatures may vary between about 32° C. and 48° C.depending on primer length. For high stringency PCR amplification, atemperature of about 62° C. is typical, although high stringencyannealing temperatures can range from about 50-65° C., depending on theprimer length and specificity. Typical cycle conditions for both highand low stringency amplifications include a denaturation phase of 90-95°C. for 30-120 sec, an annealing phase lasting 30-120 sec, and anextension phase of about 72° C. for 1-2 min. Protocols and guidelinesfor low and high stringency amplification reactions are provided, e.g.,in Innis, et al. (1990) PCR Protocols: A Guide to Methods andApplications Academic Press, N.Y.

Nucleic acids that do not hybridize to each other under stringentconditions are still substantially identical if the polypeptides whichthey encode are substantially identical. This occurs, e.g., when a copyof a nucleic acid is created using the maximum codon degeneracypermitted by the genetic code. In such cases, the nucleic acidstypically hybridize under moderately stringent hybridization conditions.Exemplary “moderately stringent hybridization conditions” include ahybridization in a buffer of 40% formamide, 1 M NaCl, 1% SDS at 37° C.,and a wash in 1×SSC at 45° C. A positive hybridization is at least twicebackground. Those of ordinary skill will readily recognize thatalternative hybridization and wash conditions can be utilized to provideconditions of similar stringency. Additional guidelines for determininghybridization parameters are provided in numerous references, e.g.,Ausubel, et al. (eds. 1991 and supplements) Current Protocols inMolecular Biology

The phrase “functional effects” in the context of assays for testingcompounds that modulate activity of a prostate cancer protein includesthe determination of a parameter that is indirectly or directly underthe influence of the prostate cancer protein or nucleic acid, e.g., afunctional, physical, or chemical effect, such as the ability todecrease prostate proliferation (malignant or non-malignant). Itincludes ligand binding activity; cell growth on soft agar; anchoragedependence; contact inhibition and density limitation of growth;cellular proliferation; cellular transformation; growth factor or serumdependence; tumor specific marker levels; invasiveness into Matrigel;tumor growth and metastasis in vivo; mRNA and protein expression incells undergoing metastasis, and other characteristics of prostatecancer cells. “Functional effects” include in vitro, in vivo, and exvivo activities.

By “determining the functional effect” is meant assaying for a compoundthat increases or decreases a parameter that is indirectly or directlyunder the influence of a prostate cancer protein sequence, e.g.,functional, enzymatic, physical and chemical effects. Such functionaleffects can be measured by means known to those skilled in the art,e.g., changes in spectroscopic characteristics (e.g., fluorescence,absorbance, refractive index), hydrodynamic (e.g., shape),chromatographic, or solubility properties for the protein, measuringinducible markers or transcriptional activation of the prostate cancerprotein; measuring binding activity or binding assays, e.g., binding toantibodies or other ligands, and measuring cellular proliferation.Determination of the functional effect of a compound on prostate cancercan also be performed using prostate cancer assays known to those ofskill in the art such as an in vitro assays, e.g., cell growth on softagar; anchorage dependence; contact inhibition and density limitation ofgrowth; cellular proliferation; cellular transformation; growth factoror serum dependence; tumor specific marker levels; invasiveness intoMatrigel; tumor growth and metastasis in vivo; mRNA and proteinexpression in cells undergoing metastasis, and other characteristics ofprostate cancer cells. The functional effects can be evaluated by manymeans known to those skilled in the art, e.g., microscopy forquantitative or qualitative measures of alterations in morphologicalfeatures, measurement of changes in RNA or protein levels for prostatecancer-associated sequences, measurement of RNA stability,identification of downstream or reporter gene expression (CAT,luciferase, β-gal, GFP, and the like), e.g., via chemiluminescence,fluorescence, colorimetric reactions, antibody binding, induciblemarkers, and ligand binding assays.

“Inhibitors”, “activators”, and “modulators” of prostate cancerpolynucleotide and polypeptide sequences are used to refer toactivating, inhibitory, or modulating molecules or compounds identifiedusing in vitro and in vivo assays of prostate cancer polynucleotide andpolypeptide sequences. Inhibitors are compounds that, e.g., bind to,partially or totally block activity, decrease, prevent, delayactivation, inactivate, desensitize, or down regulate the activity orexpression of prostate cancer proteins, e.g., antagonists. Antisensenucleic acids may seem to inhibit expression and subsequent function ofthe protein. “Activators” are compounds that increase, open, activate,facilitate, enhance activation, sensitize, agonize, or up regulateprostate cancer protein activity. Inhibitors, activators, or modulatorsalso include genetically modified versions of prostate cancer proteins,e.g., versions with altered activity, as well as naturally occurring andsynthetic ligands, antagonists, agonists, antibodies, small chemicalmolecules and the like. Such assays for inhibitors and activatorsinclude, e.g., expressing the prostate cancer protein in vitro, incells, or cell membranes, applying putative modulator compounds, andthen determining the functional effects on activity, as described above.Activators and inhibitors of prostate cancer can also be identified byincubating prostate cancer cells with the test compound and determiningincreases or decreases in the expression of 1 or more prostate cancerproteins, e.g., 1, 2, 3, 4, 5, 10, 15, 20, 25, 30, 40, 50 or moreprostate cancer proteins, such as prostate cancer proteins encoded bythe sequences set out in Tables 1A-4.

Samples or assays comprising prostate cancer proteins that are treatedwith a potential activator, inhibitor, or modulator are compared tocontrol samples without the inhibitor, activator, or modulator toexamine the extent of inhibition. Control samples (untreated withinhibitors) are assigned a relative protein activity value of 100%.Inhibition of a polypeptide is achieved when the activity value relativeto the control is about 80%, preferably 50%, more preferably 25-0%.Activation of a prostate cancer polypeptide is achieved when theactivity value relative to the control (untreated with activators) is110%, more preferably 150%, more preferably 200-500% (i.e., two to fivefold higher relative to the control), more preferably 1000-3000% higher.

The phrase “changes in cell growth” refers to a change in cell growthand proliferation characteristics in vitro or in vivo, such as cellviability, formation of foci, anchorage independence, semi-solid or softagar growth, changes in contact inhibition and density limitation ofgrowth, loss of growth factor or serum requirements, changes in cellmorphology, gaining or losing immortalization, gaining or losing tumorspecific markers, ability to form or suppress tumors when injected intosuitable animal hosts, and/or immortalization of the cell. See, e.g.,pp. 231-241 in Freshney (1994) Culture of Animal Cells: A Manual ofBasic Technique (3d ed.) Wiley-Liss.

“Tumor cell” refers to precancerous, cancerous, and/or normal cells in atumor.

“Cancer cells,” “transformed” cells, or “transformation” in tissueculture, refers to spontaneous or induced phenotypic changes that do notnecessarily involve the uptake of new genetic material. Althoughtransformation can arise from infection with a transforming virus andincorporation of new genomic DNA, or uptake of exogenous DNA, it canalso arise spontaneously or following exposure to a carcinogen, therebymutating an endogenous gene. Transformation is associated withphenotypic changes, such as immortalization of cells, aberrant growthcontrol, nonmorphological changes, and/or malignancy. See, Freshney(2001) Culture of Animal Cells: A Manual of Basic Technique (4th ed.)Wiley-Liss.

“Antibody” refers to a polypeptide comprising a framework region from animmunoglobulin gene or fragments thereof that specifically binds andrecognizes an antigen. The recognized immunoglobulin genes include thekappa, lambda, alpha, gamma, delta, epsilon, and mu constant regiongenes, as well as the myriad immunoglobulin variable region genes. Lightchains are classified as either kappa or lambda. Heavy chains areclassified as gamma, mu, alpha, delta, or epsilon, which in turn definethe immunoglobulin classes, IgG, IgM, IgA, IgD, and IgE, respectively.Typically, the antigen-binding region of an antibody or its functionalequivalent will be most critical in specificity and affinity of binding.See Paul (ed. 1999) Fundamental Immunology (4th ed.) Raven.

An exemplary immunoglobulin (antibody) structural unit comprises atetramer. Each tetramer is composed of two identical pairs ofpolypeptide chains, each pair having one “light” (about 25 kD) and one“heavy” chain (about 50-70 kD). The N-terminus of each chain defines avariable region of about 100 to 110 or more amino acids primarilyresponsible for antigen recognition. The terms variable light chain(V_(L)) and variable heavy chain (V_(H)) refer to these light and heavychains respectively.

Antibodies exist, e.g., as intact immunoglobulins or as a number ofwell-characterized fragments produced by digestion with variouspeptidases. Thus, e.g., pepsin digests an antibody below the disulfidelinkages in the hinge region to produce F(ab)′₂, a dimer of Fab whichitself is a light chain joined to V_(H)-C_(H)1 by a disulfide bond. TheF(ab)′₂ may be reduced under mild conditions to break the disulfidelinkage in the hinge region, thereby converting the F(ab)′₂ dimer intoan Fab′ monomer. The Fab′ monomer is essentially Fab with part of thehinge region (see Paul (ed. 1993) Fundamental Immunology (3d ed.) Raven.While various antibody fragments are defined in terms of the digestionof an intact antibody, one of skill will appreciate that such fragmentsmay be synthesized de novo either chemically or by using recombinant DNAmethodology. Thus, the term antibody, as used herein, also includesantibody fragments either produced by the modification of wholeantibodies, or those synthesized de novo using recombinant DNAmethodologies (e.g., single chain Fv) or those identified using phagedisplay libraries (see, e.g., McCafferty, et al. (1990) Nature348:552-554.

For preparation of antibodies, e.g., recombinant, monoclonal, orpolyclonal antibodies, many technique known in the art can be used (see,e.g., Kohler and Milstein (1975) Nature 256:495-497; Kozbor, et al.(1983) Immunology Today 4:72; pp. 77-96 in Cole, et al. (1985)Monoclonal Antibodies and Cancer Therapy Liss; Coligan (1991) CurrentProtocols in Immunology Lippincott; Harlow and Lane (1988) Antibodies: ALaboratory Manual CSH Press; and Goding (1986) Monoclonal Antibodies:Principles and Practice (2d ed.) Academic Press. Techniques for theproduction of single chain antibodies (U.S. Pat. No. 4,946,778) can beadapted to produce antibodies to polypeptides of this invention. Also,transgenic mice, or other organisms such as other mammals, may be usedto express humanized antibodies. Alternatively, phage display technologycan be used to identify antibodies and heteromeric Fab fragments thatspecifically bind to selected antigens (see, e.g., McCafferty, et al.(1990) Nature 348:552-554; Marks, et al. (1992) Biotechnology10:779-783).

A “chimeric antibody” is an antibody molecule in which (a) the constantregion, or a portion thereof, is altered, replaced or exchanged so thatthe antigen binding site (variable region) is linked to a constantregion of a different or altered class, effector function and/orspecies, or an entirely different molecule which confers new propertiesto the chimeric antibody, e.g., an enzyme, toxin, hormone, growthfactor, drug, etc.; or (b) the variable region, or a portion thereof, isaltered, replaced or exchanged with a variable region having a differentor altered antigen specificity.

Identification of Prostate Cancer-Associated Sequences

In one aspect, the expression levels of genes are determined indifferent patient samples for which diagnosis information is desired, toprovide expression profiles. An expression profile of a particularsample is essentially a “fingerprint” of the state of the sample; whiletwo states may have a particular gene similarly expressed, theevaluation of a number of genes simultaneously allows the generation ofa gene expression profile that is characteristic of the state of thecell. That is, normal tissue (e.g., normal prostate or other tissue) maybe distinguished from pathological prostate cells, e.g., cancerous ormetastatic cancerous tissue of the prostate, or prostate cancer tissueor metastatic prostate cancerous tissue can be compared with tissuesamples of prostate and other tissues from surviving cancer patients. Bycomparing expression profiles of tissue in known different prostatecancer states, information regarding which genes are important(including both up- and down-regulation of genes) in each of thesestates is obtained.

The identification of sequences that are differentially expressed inprostate cancer versus non-prostate cancer tissue allows the use of thisinformation in a number of ways. For example, a particular treatmentregime may be evaluated: does a chemotherapeutic drug act todown-regulate prostate cancer or other proliferative disorders, and thustumor growth or recurrence, in a particular patient. Alternatively, atreatment step may induce other markers which may be used as targets todestroy tumor cells. Similarly, diagnosis and treatment outcomes may bedone or confirmed by comparing patient samples with the known expressionprofiles. Maliganant disease may be compared to non-malignantconditions. Metastatic tissue can also be analyzed to determine thestage of prostate cancer in the tissue, or origin of primary tumor,e.g., metastasis from a remote primary site. Furthermore, these geneexpression profiles (or individual genes) allow screening of drugcandidates with an eye to mimicking or altering a particular expressionprofile; e.g., screening can be done for drugs that suppress theprostate cancer expression profile. This may be done by making biochipscomprising sets of the important prostate cancer genes, which can thenbe used in these screens. These methods can also be done on the proteinbasis; that is, protein expression levels of the prostate cancerproteins can be evaluated for diagnostic purposes or to screen candidateagents. In addition, the prostate cancer nucleic acid sequences can beadministered for gene therapy purposes, including the administration ofantisense nucleic acids, or the prostate cancer proteins (includingantibodies and other modulators thereof) administered as therapeuticdrugs.

Thus the present invention provides nucleic acid and protein sequencesthat are differentially expressed in prostate cancer relative to normaltissues and/or non-malignant disease, or in different types of relateddiseases, herein termed “prostate cancer sequences.” As outlined below,prostate cancer sequences include those that are up-regulated (i.e.,expressed at a higher level) in prostate cancer, as well as those thatare down-regulated (i.e., expressed at a lower level). In a preferredembodiment, the prostate cancer sequences are from humans; however, aswill be appreciated by those in the art, prostate cancer sequences fromother organisms may be useful in animal models of disease and drugevaluation; thus, other prostate cancer sequences are provided, fromvertebrates, including mammals, including rodents (rats, mice, hamsters,guinea pigs, etc.), primates, farm animals (including sheep, goats,pigs, cows, horses, etc.) and pets, e.g., (dogs, cats, etc.). Prostatecancer sequences from other organisms may be obtained using thetechniques outlined below.

Prostate cancer sequences can include both nucleic acid and amino acidsequences. As will be appreciated by those in the art and is more fullyoutlined below, prostate cancer nucleic acid sequences are useful in avariety of applications, including diagnostic applications, which willdetect naturally occurring nucleic acids, as well as screeningapplications; e.g., biochips comprising nucleic acid probes or PCRmicrotiter plates with selected probes to the prostate cancer sequencescan be generated.

A prostate cancer sequence can be initially identified by substantialnucleic acid and/or amino acid sequence homology to the prostate cancersequences outlined herein. Such homology can be based upon the overallnucleic acid or amino acid sequence, and is generally determined asoutlined below, using either homology programs or hybridizationconditions.

For identifying prostate cancer-associated sequences, the prostatecancer screen typically includes comparing genes identified in differenttissues, e.g., normal and cancerous tissues, or tumor tissue samplesfrom patients who have metastatic disease vs. non metastatic tissue.Other suitable tissue comparisons include comparing prostate cancersamples with metastatic cancer samples from other cancers, such as lung,breast, gastrointestinal cancers, ovarian, etc. Samples of differentstages of prostate cancer, e.g., survivor tissue, drug resistant states,and tissue undergoing metastasis, are applied to biochips comprisingnucleic acid probes. The samples are first microdissected, ifapplicable, and treated as is known in the art for the preparation ofmRNA. Suitable biochips are commercially available, e.g., fromAffymetrix. Gene expression profiles are generated and the dataanalyzed.

In one embodiment, the genes showing changes in expression as betweennormal and disease states are compared to genes expressed in othernormal tissues, preferably normal prostate, but also including, and notlimited to lung, heart, brain, liver, breast, kidney, muscle, colon,small intestine, large intestine, spleen, bone, and placenta. In apreferred embodiment, those genes identified during the prostate cancerscreen that are expressed in a significant amount in other tissues areremoved from the profile, although in some embodiments, this is notnecessary. That is, when screening for drugs, it is usually preferablethat the target be disease specific, to minimize possible side effectson other organs were there expression.

In a preferred embodiment, prostate cancer sequences are those that areup-regulated in prostate cancer or related conditions; that is, theexpression of these genes is higher in the prostate cancer tissue ascompared to non-cancerous tissue. “Up-regulation” as used herein oftenmeans at least about a two-fold change, preferably at least about athree fold change, with at least about five-fold or higher beingpreferred. Another embodiment is directed to sequences up-regulated innon-malignant conditions relative to normal.

Unigene cluster identification numbers and accession numbers herein arefor the GenBank sequence database and the sequences of the accessionnumbers are hereby expressly incorporated by reference. GenBank is knownin the art, see, e.g., Benson, et al. (1998) Nucleic Acids Research26:1-7 and http://www.ncbi.nlm.nih.gov/. Sequences are also available inother databases, e.g., European Molecular Biology Laboratory (EMBL) andDNA Database of Japan (DDBJ). U.S. patent application Ser. Nos.09/687,576 and 09/976,858 (-001-3) further disclose related sequences,compositions, and methods of diagnosis and treatment of prostate cancerand related conditions and are hereby expressly incorporated byreference.

In another preferred embodiment, prostate cancer sequences are thosethat are down-regulated in the prostate cancer; that is, the expressionof these genes is lower in prostate cancer tissue as compared tonon-cancerous tissue. “Down-regulation” as used herein often means atleast about a two-fold change, preferably at least about a three foldchange, with at least about five-fold or higher being preferred.

Informatics

The ability to identify genes that are over or under expressed inprostate cancer can additionally provide high-resolution,high-sensitivity datasets which can be used in the areas of diagnostics,therapeutics, drug development, pharmacogenetics, protein structure,biosensor development, and other related areas. For example, theexpression profiles can be used in diagnostic or prognostic evaluationof patients with prostate cancer. Or as another example, subcellulartoxicological information can be generated to better direct drugstructure and activity correlation (see Anderson, PharmaceuticalProteomics: Targets Mechanism, and Function, paper presented at the IBCProteomics conference, Coronado, Calif. (Jun. 11-12, 1998)). Subcellulartoxicological information can also be utilized in a biological sensordevice to predict the likely toxicological effect of chemical exposuresand likely tolerable exposure thresholds (see U.S. Pat. No. 5,811,231).Similar advantages accrue from datasets relevant to other biomoleculesand bioactive agents (e.g., nucleic acids, saccharides, lipids, drugs,and the like).

Thus, in another embodiment, the present invention provides a databasethat includes at least one set of assay data. The data contained in thedatabase is acquired, e.g., using array analysis either singly or in alibrary format. The database can be in a form in which data can bemaintained and transmitted, but is preferably an electronic database.The electronic database of the invention can be maintained on anelectronic device allowing for the storage of and access to thedatabase, such as a personal computer, but is preferably distributed ona wide area network, such as the World Wide Web.

The focus of the present section on databases that include peptidesequence data is for clarity of illustration only. It will be apparentto those of skill in the art that similar databases can be assembled forassay data acquired using an assay of the invention.

The compositions and methods for identifying and/or quantitating therelative and/or absolute abundance of a variety of molecular andmacromolecular species from a biological sample undergoing prostatecancer, i.e., the identification of prostate cancer-associated sequencesdescribed herein, provide an abundance of information, which can becorrelated with pathological conditions, predisposition to disease, drugtesting, therapeutic monitoring, gene-disease causal linkages,identification of correlates of immunity and physiological status, amongothers. Although the data generated from the assays of the invention issuited for manual review and analysis, in a preferred embodiment, priordata processing using high-speed computers is utilized.

An array of methods for indexing and retrieving biomolecular informationis known in the art. For example, U.S. Pat. Nos. 6,023,659 and 5,966,712disclose a relational database system for storing biomolecular sequenceinformation in a manner that allows sequences to be catalogued andsearched according to one or more protein function hierarchies. U.S.Pat. No. 5,953,727 discloses a relational database having sequencerecords containing information in a format that allows a collection ofpartial-length DNA sequences to be catalogued and searched according toassociation with one or more sequencing projects for obtainingfull-length sequences from the collection of partial length sequences.U.S. Pat. No. 5,706,498 discloses a gene database retrieval system formaking a retrieval of a gene sequence similar to a sequence data item ina gene database based on the degree of similarity between a key sequenceand a target sequence. U.S. Pat. No. 5,538,897 discloses a method usingmass spectroscopy fragmentation patterns of peptides to identify aminoacid sequences in computer databases by comparison of predicted massspectra with experimentally-derived mass spectra using acloseness-of-fit measure. U.S. Pat. No. 5,926,818 discloses amulti-dimensional database comprising a functionality formulti-dimensional data analysis described as on-line analyticalprocessing (OLAP), which entails the consolidation of projected andactual data according to more than one consolidation path or dimension.U.S. Pat. No. 5,295,261 reports a hybrid database structure in which thefields of each database record are divided into two classes,navigational and informational data, with navigational fields stored ina hierarchical topological map which can be viewed as a tree structureor as the merger of two or more such tree structures.

See also Mount, et al. (2001) Bioinformatics CSH Press; Durbin, et al.(eds. 1999) Biological Sequence Analysis: Probabilistic Models ofProteins and Nucleic Acids Cambridge Univ. Press; Baxevanis andOeullette (eds., 1998) Bioinformatics: A Practical Guide to the Analysisof Genes and Proteins Wiley-Liss; Rashidi and Buehler (1999)Bioinformatics: Basic Applications in Biological Science and MedicineCRC Press; Setubal, et al. (eds. 1997) Introduction to ComputationalMolecular Biology Brooks/Cole; Misener and Krawetz (eds. 2000)Bioinformatics: Methods and Protocols Human Press; Higgins and Taylor(eds. 2000) Bioinformatics: Sequence, Structure, and Databanks: APractical Approach Oxford Univ. Press; Brown (2001) Bioinformatics: ABiologist's Guide to Biocomputing and the Internet Eaton Pub; Han andKamber (2000) Data Mining: Concepts and Techniques Kaufmann Pub.; andWaterman (1995) Introduction to Computational Biology: Maps, Sequences,and Genomes Chap and Hall.

The present invention provides a computer database comprising a computerand software for storing in computer-retrievable form assay data recordscross-tabulated, e.g., with data specifying the source of thetarget-containing sample from which each sequence specificity record wasobtained.

In an exemplary embodiment, at least one of the sources oftarget-containing sample is from a control tissue sample known to befree of pathological disorders. In a variation, at least one of thesources is a known pathological tissue specimen, e.g., a neoplasticlesion or another tissue specimen to be analyzed for prostate cancer. Inanother variation, the assay records cross-tabulate one or more of thefollowing parameters for each target species in a sample: (1) a uniqueidentification code, which can include, e.g., a target molecularstructure and/or characteristic separation coordinate (e.g.,electrophoretic coordinates); (2) sample source; and (3) absolute and/orrelative quantity of the target species present in the sample.

The invention also provides for the storage and retrieval of acollection of target data in a computer data storage apparatus, whichcan include magnetic disks, optical disks, magneto-optical disks, DRAM,SRAM, SGRAM, SDRAM, RDRAM, DDR RAM, magnetic bubble memory devices, andother data storage devices, including CPU registers and on-CPU datastorage arrays. Typically, the target data records are stored as a bitpattern in an array of magnetic domains on a magnetizable medium or asan array of charge states or transistor gate states, such as an array ofcells in a DRAM device (e.g., each cell comprised of a transistor and acharge storage area, which may be on the transistor). In one embodiment,the invention provides such storage devices, and computer systems builttherewith, comprising a bit pattern encoding a protein expressionfingerprint record comprising unique identifiers for at least 10 targetdata records cross-tabulated with target source.

When the target is a peptide or nucleic acid, the invention preferablyprovides a method for identifying related peptide or nucleic acidsequences, comprising performing a computerized comparison between apeptide or nucleic acid sequence assay record stored in or retrievedfrom a computer storage device or database and at least one othersequence. The comparison can include a sequence analysis or comparisonalgorithm or computer program embodiment thereof (e.g., FASTA, TFASTA,GAP, BESTFIT) and/or the comparison may be of the relative amount of apeptide or nucleic acid sequence in a pool of sequences determined froma polypeptide or nucleic acid sample of a specimen.

The invention also preferably provides a magnetic disk, such as anIBM-compatible (DOS, Windows, Windows95/98/2000, Windows NT, OS/2) orother format (e.g., Linux, SunOS, Solaris, AIX, SCO Unix, VMS, MV,Macintosh, etc.) floppy diskette or hard (fixed, Winchester) disk drive,comprising a bit pattern encoding data from an assay of the invention ina file format suitable for retrieval and processing in a computerizedsequence analysis, comparison, or relative quantitation method.

The invention also provides a network, comprising a plurality ofcomputing devices linked via a data link, such as an Ethernet cable(coax or 10BaseT), telephone line, ISDN line, wireless network, opticalfiber, or other suitable signal transmission medium, whereby at leastone network device (e.g., computer, disk array, etc.) comprises apattern of magnetic domains (e.g., magnetic disk) and/or charge domains(e.g., an array of DRAM cells) composing a bit pattern encoding dataacquired from an assay of the invention.

The invention also provides a method for transmitting assay data thatincludes generating an electronic signal on an electronic communicationsdevice, such as a modem, ISDN terminal adapter, DSL, cable modem, ATMswitch, or the like, wherein the signal includes (in native or encryptedformat) a bit pattern encoding data from an assay or a databasecomprising a plurality of assay results obtained by the method of theinvention.

In a preferred embodiment, the invention provides a computer system forcomparing a query target to a database containing an array of datastructures, such as an assay result obtained by the method of theinvention, and ranking database targets based on the degree of identityand gap weight to the target data. A central processor is preferablyinitialized to load and execute the computer program for alignmentand/or comparison of the assay results. Data for a query target isentered into the central processor via an I/O device. Execution of thecomputer program results in the central processor retrieving the assaydata from the data file, which comprises a binary description of anassay result.

The target data or record and the computer program can be transferred tosecondary memory, which is typically random access memory (e.g., DRAM,SRAM, SGRAM, or SDRAM). Targets are ranked according to the degree ofcorrespondence between a selected assay characteristic (e.g., binding toa selected affinity moiety) and the same characteristic of the querytarget and results are output via an I/O device. For example, a centralprocessor can be a conventional computer (e.g., Intel Pentium, PowerPC,Alpha, PA-8000, SPARC, MIPS 4400, MIPS 10000, VAX, etc.); a program canbe a commercial or public domain molecular biology software package(e.g., UWGCG Sequence Analysis Software, Darwin); a data file can be anoptical or magnetic disk, a data server, a memory device (e.g., DRAM,SRAM, SGRAM, SDRAM, EPROM, bubble memory, flash memory, etc.); an I/Odevice can be a terminal comprising a video display and a keyboard, amodem, an ISDN terminal adapter, an Ethernet port, a punched cardreader, a magnetic strip reader, or other suitable I/O device.

The invention also preferably provides the use of a computer system,such as that described above, which comprises: (1) a computer; (2) astored bit pattern encoding a collection of peptide sequence specificityrecords obtained by the methods of the invention, which may be stored inthe computer; (3) a comparison target, such as a query target; and (4) aprogram for alignment and comparison, typically with rank-ordering ofcomparison results on the basis of computed similarity values.

Characteristics of Prostate Cancer-Associated Proteins

Prostate cancer proteins of the present invention may be classified assecreted proteins, transmembrane proteins, or intracellular proteins. Inone embodiment, the prostate cancer protein is an intracellular protein.Intracellular proteins may be found in the cytoplasm and/or in thenucleus. Intracellular proteins are involved in all aspects of cellularfunction and replication (including, e.g., signaling pathways); aberrantexpression of such proteins often results in unregulated or disregulatedcellular processes (see, e.g., Alberts (ed. 1994) Molecular Biology ofthe Cell (3d ed.) Garland. For example, many intracellular proteins haveenzymatic activity such as protein kinase activity, protein phosphataseactivity, protease activity, nucleotide cyclase activity, polymeraseactivity and the like. Intracellular proteins also serve as dockingproteins that are involved in organizing complexes of proteins, ortargeting proteins to various subcellular localizations, and areinvolved in maintaining the structural integrity of organelles.

An increasingly appreciated concept in characterizing proteins is thepresence in the proteins of one or more structural motifs for whichdefined functions have been attributed. In addition to the highlyconserved sequences found in the enzymatic domain of proteins, highlyconserved sequences have been identified in proteins that are involvedin protein-protein interaction. For example, Src-homology-2 (SH2)domains bind tyrosine-phosphorylated targets in a sequence dependentmanner. PTB domains, which are distinct from SH2 domains, also bindtyrosine phosphorylated targets. SH3 domains bind to proline-richtargets. In addition, PH domains, tetratricopeptide repeats and WDdomains to name only a few, have been shown to mediate protein-proteininteractions. Some of these may also be involved in binding tophospholipids or other second messengers. As will be appreciated by oneof ordinary skill in the art, these motifs can be identified on thebasis of amino acid sequence; thus, an analysis of the sequence ofproteins may provide insight into both the enzymatic potential of themolecule and/or molecules with which the protein may associate. Oneuseful database is Pfam (protein families), which is a large collectionof multiple sequence alignments and hidden Markov models covering manycommon protein domains. Versions are available via the internet fromWashington University in St. Louis, the Sanger Center in England, andthe Karolinska Institute in Sweden (see, e.g., Bateman, et al. (2000)Nuc. Acids Res. 28:263-266; Sonnhammer, et al. (1997) Proteins28:405-420; Bateman, et al. (1999) Nuc. Acids Res. 27:260-262; andSonnhammer, et al. (1998) Nuc. Acids Res. 26:320-322.

In another embodiment, the prostate cancer sequences are transmembraneproteins. Transmembrane proteins are molecules that span a phospholipidbilayer of a cell. They may have an intracellular domain, anextracellular domain, or both. The intracellular domains of suchproteins may have a number of functions including those alreadydescribed for intracellular proteins. For example, the intracellulardomain may have enzymatic activity and/or may serve as a binding sitefor additional proteins. Frequently the intracellular domain oftransmembrane proteins serves both roles. For example certain receptortyrosine kinases have both protein kinase activity and SH2 domains. Inaddition, autophosphorylation of tyrosines on the receptor moleculeitself, creates binding sites for additional SH2 domain containingproteins.

Transmembrane proteins may contain from one to many transmembranedomains. For example, receptor tyrosine kinases, certain cytokinereceptors, receptor guanylyl cyclases and receptor serine/threonineprotein kinases contain a single transmembrane domain. However, variousother proteins including channels and adenylyl cyclases contain numeroustransmembrane domains. Many important cell surface receptors such as Gprotein coupled receptors (GPCRs) are classified as “seven transmembranedomain” proteins, as they contain 7 membrane spanning regions.Characteristics of transmembrane domains include approximately 17consecutive hydrophobic amino acids that may be followed by chargedamino acids. Therefore, upon analysis of the amino acid sequence of aparticular protein, the localization and number of transmembrane domainswithin the protein may be predicted (see, e.g., PSORT web sitehttp://psort.nibb.ac.jp/). Important transmembrane-protein receptorsinclude, but are not limited to the insulin receptor, insulin-likegrowth factor receptor, human growth hormone receptor, glucosetransporters, transferrin receptor, epidermal growth factor receptor,low density lipoprotein receptor, epidermal growth factor receptor,leptin receptor, and interleukin receptors, e.g., IL-1 receptor, IL-2receptor, etc.

The extracellular domains of transmembrane proteins are diverse;however, conserved motifs are found repeatedly among variousextracellular domains. Conserved structure and/or functions have beenascribed to different extracellular motifs. Many extracellular domainsare involved in binding to other molecules. In one aspect, extracellulardomains are found on receptors. Factors that bind the receptor domaininclude circulating ligands, which may be peptides, proteins, or smallmolecules such as adenosine and the like. For example, growth factorssuch as EGF, FGF, and PDGF are circulating growth factors that bind totheir cognate receptors to initiate a variety of cellular responses.Other factors include cytokines, mitogenic factors, neurotrophic factorsand the like. Extracellular domains also bind to cell-associatedmolecules. In this respect, they mediate cell-cell interactions.Cell-associated ligands can be tethered to the cell, e.g., via aglycosylphosphatidylinositol (GPI) anchor, or may themselves betransmembrane proteins. Extracellular domains also associate with theextracellular matrix and contribute to the maintenance of the cellstructure.

Prostate cancer proteins that are transmembrane are particularlypreferred in the present invention as they are readily accessibletargets for immunotherapeutics, as are described herein. In addition, asoutlined below, transmembrane proteins can be also useful in imagingmodalities. Antibodies may be used to label such readily accessibleproteins in situ. Alternatively, antibodies can also label intracellularproteins, in which case samples are typically permeabilized to provideaccess to intracellular proteins. In addition, some membrane proteinscan be processed to release a soluble protein, or to expose a residualfragment. Released soluble proteins may be useful diagnostic markers,processed residual protein fragments may be useful prostate markers ofdisease.

It will also be appreciated by those in the art that a transmembraneprotein can be made soluble by removing transmembrane sequences, e.g.,through recombinant methods. Furthermore, transmembrane proteins thathave been made soluble can be made to be secreted through recombinantmeans by adding an appropriate signal sequence.

In another embodiment, the prostate cancer proteins are secretedproteins; the secretion of which can be either constitutive orregulated. These proteins may have a signal peptide or signal sequencethat targets the molecule to the secretory pathway. Secreted proteinsare involved in numerous physiological events; by virtue of theircirculating nature, they often serve to transmit signals to variousother cell types. The secreted protein may function in an autocrinemanner (acting on the cell that secreted the factor), a paracrine manner(acting on cells in close proximity to the cell that secreted thefactor), an endocrine manner (acting on cells at a distance, e.g,secretion into the blood stream), or an exocrine manner (secretion,e.g., through a duct or to adjacent epithelial surface as sweat glands,sebaceous glands, pancreatic ducts, lacrimal glands, mammary glands, saxproducing glands of the ear, etc.). Thus secreted molecules find use inmodulating or altering numerous aspects of physiology. Prostate cancerproteins that are secreted proteins are particularly preferred in thepresent invention as they serve as good targets for diagnostic markers,e.g., for blood, plasma, serum, or stool tests. Those which are enzymesmay be antibody or small molecule targets. Others may be useful asvaccine targets, e.g., via CTL mechanisms.

Use of Prostate Cancer Nucleic Acids

As described above, prostate cancer sequence is initially identified bysubstantial nucleic acid and/or amino acid sequence homology or linkageto the prostate cancer sequences outlined herein. Such homology can bebased upon the overall nucleic acid or amino acid sequence, and isgenerally determined as outlined below, using either homology programsor hybridization conditions. Typically, linked sequences on a mRNA arefound on the same molecule.

The prostate cancer nucleic acid sequences of the invention, e.g., thesequences in Tables 1A-4, can be fragments of larger genes, i.e., theyare nucleic acid segments. “Genes” in this context includes codingregions, non-coding regions, and mixtures of coding and non-codingregions. Accordingly, as will be appreciated by those in the art, usingthe sequences provided herein, extended sequences, in either direction,of the prostate cancer genes can be obtained, using techniques wellknown in the art for cloning either longer sequences or the full lengthsequences; see Ausubel, et al., supra. Much can be done by informaticsand many sequences can be clustered to include multiple sequencescorresponding to a single gene, e.g., systems such as UniGene (see,http://www.ncbi.nlm.nih.gov/UniGene/).

Once the prostate cancer nucleic acid is identified, it can be clonedand, if necessary, its constituent parts recombined to form the entireprostate cancer nucleic acid coding regions or the entire mRNA sequence.Once isolated from its natural source, e.g., contained within a plasmidor other vector or excised therefrom as a linear nucleic acid segment,the recombinant prostate cancer nucleic acid can be further-used as aprobe to identify and isolate other prostate cancer nucleic acids, e.g.,extended coding regions. It can also be used as a “precursor” nucleicacid to make modified or variant prostate cancer nucleic acids andproteins.

The prostate cancer nucleic acids of the present invention are used inseveral ways. In a first embodiment, nucleic acid probes to the prostatecancer nucleic acids are made and attached to biochips to be used inscreening and diagnostic methods, as outlined below, or foradministration, e.g., for gene therapy, vaccine, and/or antisenseapplications. Alternatively, the prostate cancer nucleic acids thatinclude coding regions of prostate cancer proteins can be put intoexpression vectors for the expression of prostate cancer proteins, againfor screening purposes or for administration to a patient.

In a preferred embodiment, nucleic acid probes to prostate cancernucleic acids (both the nucleic acid sequences outlined in the figuresand/or the complements thereof) are made. The nucleic acid probesattached to the biochip are designed to be substantially complementaryto the prostate cancer nucleic acids, i.e., the target sequence (eitherthe target sequence of the sample or to other probe sequences, e.g., insandwich assays), such that hybridization of the target sequence and theprobes of the present invention occurs. As outlined below, thiscomplementarity need not be perfect; there may be base pair mismatcheswhich will interfere with hybridization between the target sequence andthe single stranded nucleic acids of the present invention. However, ifthe number of mutations is so great that no hybridization can occurunder even the least stringent of hybridization conditions, the sequenceis not a complementary target sequence. Thus, by “substantiallycomplementary” herein is meant that the probes are sufficientlycomplementary to the target sequences to hybridize under normal reactionconditions, particularly high stringency conditions, as outlined herein.

A nucleic acid probe is generally single stranded but can be partiallysingle and partially double stranded. The strandedness of the probe isdictated by the structure, composition, and properties of the targetsequence. In general, the nucleic acid probes range from about 8 toabout 100 bases long, with from about 10 to about 80 bases beingpreferred, and from about 30 to about 50 bases being particularlypreferred. That is, generally whole genes are not used. In someembodiments, much longer nucleic acids can be used, up to hundreds ofbases.

In a preferred embodiment, more than one probe per sequence is used,with either overlapping probes or probes to different sections of thetarget being used. That is, two, three, four or more probes, with threebeing preferred, are used to build in a redundancy for a particulartarget. The probes can be overlapping (i.e., have some sequence incommon), or separate. In some cases, PCR primers may be used to amplifysignal for higher sensitivity.

As will be appreciated by those in the art, nucleic acids can beattached or immobilized to a solid support in a wide variety of ways. By“immobilized” and grammatical equivalents herein is meant theassociation or binding between the nucleic acid probe and the solidsupport is sufficient to be stable under the conditions of binding,washing, analysis, and removal as outlined below. The binding cantypically be covalent or non-covalent. By “non-covalent binding” andgrammatical equivalents herein is meant one or more of electrostatic,hydrophilic, and hydrophobic interactions. Included in non-covalentbinding is the covalent attachment of a molecule, such as, streptavidinto the support and the non-covalent binding of the biotinylated probe tothe streptavidin. By “covalent binding” and grammatical equivalentsherein is meant that the two moieties, the solid support and the probe,are attached by at least one bond, including sigma bonds, pi bonds andcoordination bonds. Covalent bonds can be formed directly between theprobe and the solid support or can be formed by a cross linker or byinclusion of a specific reactive group on either the solid support orthe probe or both molecules. Immobilization may also involve acombination of covalent and non-covalent interactions.

In general, the probes are attached to the biochip in a wide variety ofways, as will be appreciated by those in the art. As described herein,the nucleic acids can either be synthesized first, with subsequentattachment to the biochip, or can be directly synthesized on thebiochip.

The biochip comprises a suitable solid substrate. By “substrate” or“solid support” or other grammatical equivalents herein is meant amaterial that can be modified to contain discrete individual sitesappropriate for the attachment or association of the nucleic acid probesand is amenable to at least one detection method. As will be appreciatedby those in the art, the number of possible substrates are very large,and include, but are not limited to, glass and modified orfunctionalized glass, plastics (including acrylics, polystyrene andcopolymers of styrene and other materials, polypropylene, polyethylene,polybutylene, polyurethanes, TeflonJ, etc.), polysaccharides, nylon ornitrocellulose, resins, silica or silica-based materials includingsilicon and modified silicon, carbon, metals, inorganic glasses,plastics, etc. In general, the substrates allow optical detection and donot appreciably fluoresce. A preferred substrate is described inWO0055627, herein incorporated by reference in its entirety.

Generally the substrate is planar, although as will be appreciated bythose in the art, other configurations of substrates may be used aswell. For example, the probes may be placed on the inside surface of atube, for flow-through sample analysis to minimize sample volume.Similarly, the substrate may be flexible, such as a flexible foam,including closed cell foams made of particular plastics.

In a preferred embodiment, the surface of the biochip and the probe maybe derivatized with chemical functional groups for subsequent attachmentof the two. Thus, e.g., the biochip is derivatized with a chemicalfunctional group including, but not limited to, amino groups, carboxygroups, oxo groups and thiol groups, with amino groups beingparticularly preferred. Using these functional groups, the probes can beattached using functional groups on the probes. For example, nucleicacids containing amino groups can be attached to surfaces comprisingamino groups, e.g., using linkers as are known in the art; e.g., homo-or hetero-bifunctional linkers as are well known (see 1994 PierceChemical Company catalog, technical section on cross-linkers, pages155-200). In addition, in some cases, additional linkers, such as alkylgroups (including substituted and heteroalkyl groups) may be used.

In this embodiment, oligonucleotides are synthesized as is known in theart, and then attached to the surface of the solid support. As will beappreciated by those skilled in the art, either the 5′ or 3′ terminusmay be attached to the solid support, or attachment may be via aninternal nucleoside.

In another embodiment, the immobilization to the solid support may bevery strong, yet non-covalent. For example, biotinylatedoligonucleotides can be made, which bind to surfaces covalently coatedwith streptavidin, resulting in attachment.

Alternatively, the oligonucleotides may be synthesized on the surface,as is known in the art. For example, photoactivation techniquesutilizing photopolymerization compounds and techniques are used. In apreferred embodiment, the nucleic acids can be synthesized in situ,using well known photolithographic techniques, such as those describedin WO 95/25116; WO 95/35505; U.S. Pat. Nos. 5,700,637 and 5,445,934; andreferences cited within, all of which are expressly incorporated byreference; these methods of attachment form the basis of the AffymetrixGeneChip™ technology.

Often, amplification-based assays are performed to measure theexpression level of prostate cancer-associated sequences. These assaysare typically performed in conjunction with reverse transcription. Insuch assays, a prostate cancer-associated nucleic acid sequence acts asa template in an amplification reaction (e.g., Polymerase ChainReaction, or PCR). In a quantitative amplification, the amount ofamplification product will be proportional to the amount of template inthe original sample. Comparison to appropriate controls provides ameasure of the amount of prostate cancer-associated RNA. Methods ofquantitative amplification are well known to those of skill in the art.Detailed protocols for quantitative PCR are provided, e.g., in Innis, etal. (1990) PCR Protocols: A Guide to Methods and Applications AcademicPress.

In some embodiments, a TaqMan based assay is used to measure expression.TaqMan based assays use a fluorogenic oligonucleotide probe thatcontains a 5′ fluorescent dye and a 3′ quenching agent. The probehybridizes to a PCR product, but cannot itself be extended due to ablocking agent at the 3′ end. When the PCR product is amplified insubsequent cycles, the 5′ nuclease activity of the polymerase, e.g.,AmpliTaq, results in the cleavage of the TaqMan probe. This cleavageseparates the 5′ fluorescent dye and the 3′ quenching agent, therebyresulting in an increase in fluorescence as a function of amplification(see, e.g., literature provided by Perkin-Elmer, e.g.,www2.perkin-elmer.com).

Other suitable amplification methods include, but are not limited to,ligase chain reaction (LCR) (see Wu and Wallace (1989) Genomics4:560-569, Landegren, et al. (1988) Science 241:1077-1080, andBarringer, et al. (1990) Gene 89:117-122), transcription amplification(Kwoh, et al. (1989) Proc. Natl. Acad. Sci. USA 86:1173-1177),self-sustained sequence replication (Guatelli, et al. (1990) Proc. Nat.Acad. Sci. USA 87:1874-1878), dot PCR, and linker adapter PCR, etc.

Expression of Prostate Cancer Proteins from Nucleic Acids

In a preferred embodiment, prostate cancer nucleic acids, e.g., encodingprostate cancer proteins are used to make a variety of expressionvectors to express prostate cancer proteins which can then be used inscreening assays, as described below. Expression vectors and recombinantDNA technology are well known to those of skill in the art (see, e.g.,Ausubel, supra, and Fernandez and Hoeffler (eds. 1999) Gene ExpressionSystems Academic Press) and are used to express proteins. The expressionvectors may be either self-replicating extrachromosomal vectors orvectors which integrate into a host genome. Generally, these expressionvectors include transcriptional and translational regulatory nucleicacid operably linked to the nucleic acid encoding the prostate cancerprotein. The term “control sequences” refers to DNA sequences used forthe expression of an operably linked coding sequence in a particularhost organism. Control sequences that are suitable for prokaryotes,e.g., include a promoter, optionally an operator sequence, and aribosome binding site. Eukaryotic cells are known to utilize promoters,polyadenylation signals, and enhancers.

Nucleic acid is “operably linked” when it is placed into a functionalrelationship with another nucleic acid sequence. For example, DNA for apresequence or secretory leader is operably linked to DNA for apolypeptide if it is expressed as a preprotein that participates in thesecretion of the polypeptide; a promoter or enhancer is operably linkedto a coding sequence if it affects the transcription of the sequence; aribosome binding site is operably linked to a coding sequence if it ispositioned so as to facilitate translation, and sequences may beoperably linked when they are physically linked on the same molecule.Generally, “operably linked” means that the DNA sequences being linkedare contiguous, and, in the case of a secretory leader, contiguous andin reading phase. However, enhancers do not have to be contiguous.Linking is typically accomplished by ligation at convenient restrictionsites. If such sites do not exist, synthetic oligonucleotide adaptors orlinkers are used in accordance with conventional practice.Transcriptional and translational regulatory nucleic acid will generallybe appropriate to the host cell used to express the prostate cancerprotein. Numerous types of appropriate expression vectors, and suitableregulatory sequences are known in the art for a variety of host cells.

In general, transcriptional and translational regulatory sequences mayinclude, but are not limited to, promoter sequences, ribosomal bindingsites, transcriptional start and stop sequences, translational start andstop sequences, and enhancer or activator sequences. In a preferredembodiment, the regulatory sequences include a promoter andtranscriptional start and stop sequences.

Promoter sequences encode either constitutive or inducible promoters.The promoters may be either naturally occurring promoters or hybridpromoters. Hybrid promoters, which combine elements of more than onepromoter, are also known in the art, and are useful in the presentinvention.

In addition, an expression vector may comprise additional elements. Forexample, the expression vector may have two replication systems, thusallowing it to be maintained in two organisms, e.g., in mammalian orinsect cells for expression and in a prokaryotic host for cloning andamplification. Furthermore, for integrating expression vectors, theexpression vector contains at least one sequence homologous to the hostcell genome, and preferably two homologous sequences which flank theexpression construct. The integrating vector may be directed to aspecific locus in the host cell by selecting the appropriate homologoussequence for inclusion in the vector. Constructs for integrating vectorsare well known in the art (e.g., Fernandez and Hoeffler, supra).

In addition, in a preferred embodiment, the expression vector contains aselectable marker gene to allow the selection of transformed host cells.Selection genes are well known in the art and will vary with the hostcell used.

The prostate cancer proteins of the present invention are produced byculturing a host cell transformed with an expression vector containingnucleic acid encoding a prostate cancer protein, under the appropriateconditions to induce or cause expression of the prostate cancer protein.Conditions appropriate for prostate cancer protein expression will varywith the choice of the expression vector and the host cell, and will beeasily ascertained by one skilled in the art through routineexperimentation or optimization. For example, the use of constitutivepromoters in the expression vector will require optimizing the growthand proliferation of the host cell, while the use of an induciblepromoter requires the appropriate growth conditions for induction. Inaddition, in some embodiments, the timing of the harvest is important.For example, the baculoviral systems used in insect cell expression arelytic viruses, and thus harvest time selection can be crucial forproduct yield.

Appropriate host cells include yeast, bacteria, archaebacteria, fungi,and insect and animal cells, including mammalian cells. Of particularinterest are Saccharomyces cerevisiae and other yeasts, E. coli,Bacillus subtilis, Sf9 cells, C129 cells, 293 cells, Neurospora, BHK,CHO, COS, HeLa cells, HUVEC (human umbilical vein endothelial cells),THP1 cells (a macrophage cell line) and various other human cells andcell lines.

In a preferred embodiment, the prostate cancer proteins are expressed inmammalian cells. Mammalian expression systems are also known in the art,and include retroviral and adenoviral systems. One expression vectorsystem is a retroviral vector system such as is generally described inPCT/US97/01019 and PCT/US97/01048, both of which are hereby expresslyincorporated by reference. Of particular use as mammalian promoters arethe promoters from mammalian viral genes, since the viral genes areoften highly expressed and have a broad host range. Examples include theSV40 early promoter, mouse mammary tumor virus LTR promoter, adenovirusmajor late promoter, herpes simplex virus promoter, and the CMV promoter(see, e.g., Fernandez and Hoeffler, supra). Typically, transcriptiontermination and polyadenylation sequences recognized by mammalian cellsare regulatory regions located 3′ to the translation stop codon andthus, together with the promoter elements, flank the coding sequence.Examples of transcription terminator and polyadenylation signals includethose derived form SV40.

The methods of introducing exogenous nucleic acid into mammalian hosts,as well as other hosts, is well known in the art, and will vary with thehost cell used. Techniques include dextran-mediated transfection,calcium phosphate precipitation, polybrene mediated transfection,protoplast fusion, electroporation, viral infection, encapsulation ofthe polynucleotide(s) in liposomes, and direct microinjection of the DNAinto nuclei.

In a preferred embodiment, prostate cancer proteins are expressed inbacterial systems. Bacterial expression systems are well known in theart. Promoters from bacteriophage may also be used and are known in theart. In addition, synthetic promoters and hybrid promoters are alsouseful; e.g., the tac promoter is a hybrid of the trp and lac promotersequences. Furthermore, a bacterial promoter can include naturallyoccurring promoters of non-bacterial origin that have the ability tobind bacterial RNA polymerase and initiate transcription. In addition toa functioning promoter sequence, an efficient ribosome binding site isdesirable. The expression vector may also include a signal peptidesequence that provides for secretion of the prostate cancer protein inbacteria. The protein is either secreted into the growth media(gram-positive bacteria) or into the periplasmic space, located betweenthe inner and outer membrane of the cell (gram-negative bacteria). Thebacterial expression vector may also include a selectable marker gene toallow for the selection of bacterial strains that have been transformed.Suitable selection genes include genes which render the bacteriaresistant to drugs such as ampicillin, chloramphenicol, erythromycin,kanamycin, neomycin and tetracycline. Selectable markers also includebiosynthetic genes, such as those in the histidine, tryptophan andleucine biosynthetic pathways. These components are assembled intoexpression vectors. Expression vectors for bacteria are well known inthe art, and include vectors for Bacillus subtilis, E. coli,Streptococcus cremoris, and Streptococcus lividans, among others (e.g.,Fernandez and Hoeffler, supra). The bacterial expression vectors aretransformed into bacterial host cells using techniques well known in theart, such as calcium chloride treatment, electroporation, and others.

In one embodiment, prostate cancer proteins are produced in insectcells. Expression vectors for the transformation of insect cells, and inparticular, baculovirus-based expression vectors, are well known in theart.

In a preferred embodiment, prostate cancer protein is produced in yeastcells. Yeast expression systems are well known in the art, and includeexpression vectors for Saccharomyces cerevisiae, Candida albicans and C.maltosa, Hansenula polymorpha, Kluyveromyces fragilis and K. lactis,Pichia guillerimondii and P. pastoris, Schizosaccharomyces pombe, andYarrowia lipolytica.

The prostate cancer protein may also be made as a fusion protein, usingtechniques well known in the art. Thus, e.g., for the creation ofmonoclonal antibodies, if the desired epitope is small, the prostatecancer protein may be fused to a carrier protein to form an immunogen.Alternatively, the prostate cancer protein may be made as a fusionprotein to increase expression, or for other reasons. For example, whenthe prostate cancer protein is a prostate cancer peptide, the nucleicacid encoding the peptide may be linked to other nucleic acid forexpression purposes.

In a preferred embodiment, the prostate cancer protein is purified orisolated after expression. Prostate cancer proteins may be isolated orpurified in a variety of ways known to those skilled in the artdepending on what other components are present in the sample. Standardpurification methods include electrophoretic, molecular, immunologicaland chromatographic techniques, including ion exchange, hydrophobic,affinity, and reverse-phase HPLC chromatography, and chromatofocusing.For example, the prostate cancer protein may be purified using astandard anti-prostate cancer protein antibody column. Ultrafiltrationand diafiltration techniques, in conjunction with protein concentration,are also useful. For general guidance in suitable purificationtechniques, see Scopes (1982) Protein Purification Springer-Verlag. Thedegree of purification necessary will vary depending on the use of theprostate cancer protein. In some instances no purification will benecessary.

Once expressed and purified if necessary, the prostate cancer proteinsand nucleic acids are useful in a number of applications. They may beused as immunoselection reagents, as vaccine reagents, as screeningagents, etc.

Variants of Prostate Cancer Proteins

In one embodiment, the prostate cancer proteins are derivative orvariant prostate cancer proteins as compared to the wild-type sequence.That is, as outlined more fully below, the derivative prostate cancerpeptide will often contain at least one amino acid substitution,deletion or insertion, with amino acid substitutions being particularlypreferred. The amino acid substitution, insertion, or deletion may occurat most any residue within the prostate cancer peptide.

Also included within one embodiment of prostate cancer proteins of thepresent invention are amino acid sequence variants. These variantstypically fall into one or more of three classes: substitutional,insertional, or deletional variants. These variants ordinarily areprepared by site specific mutagenesis of nucleotides in the DNA encodingthe prostate cancer protein, using cassette or PCR mutagenesis or othertechniques well known in the art, to produce DNA encoding the variant,and thereafter expressing the DNA in recombinant cell culture asoutlined above. However, variant prostate cancer protein fragmentshaving up to about 100-150 residues may be prepared by in vitrosynthesis using established techniques. Amino acid sequence variants arecharacterized by the predetermined nature of the variation, a featurethat sets them apart from naturally occurring allelic or interspeciesvariation of the prostate cancer protein amino acid sequence. Thevariants typically exhibit the same qualitative biological activity asthe naturally occurring analogue, although variants can also be selectedwhich have modified characteristics as will be more fully outlinedbelow.

While the site or region for introducing an amino acid sequencevariation is predetermined, the mutation per se need not bepredetermined. For example, in order to optimize the performance of amutation at a given site, random mutagenesis may be conducted at thetarget codon or region and the expressed prostate cancer variantsscreened for the optimal combination of desired activity. Techniques formaking substitution mutations at predetermined sites in DNA having aknown sequence are well known, e.g., M13 primer mutagenesis and PCRmutagenesis. Screening of the mutants is done using assays of prostatecancer protein activities.

Amino acid substitutions are typically of single residues, insertionsusually will be on the order of from about 1 to 20 amino acids, althoughconsiderably larger insertions may be tolerated. Deletions range fromabout 1 to about 20 residues, although in some cases deletions may bemuch larger.

Substitutions, deletions, insertions or a combination thereof may beused to arrive at a final derivative. Generally these changes are doneon a few amino acids to minimize the alteration of the molecule.However, larger changes may be tolerated in certain circumstances. Whensmall alterations in the characteristics of the prostate cancer proteinare desired, substitutions are generally made in accordance with theamino acid substitution relationships provided in the definitionsection.

The variants typically exhibit the same qualitative biological activityand will elicit the same immune response as the naturally-occurringanalog, although variants also are selected to modify thecharacteristics of the prostate cancer proteins as needed.Alternatively, the variant may be designed such that the biologicalactivity of the prostate cancer protein is altered. For example,glycosylation sites may be altered or removed.

Substantial changes in function or immunological identity are made byselecting substitutions that are less conservative than those describedabove. For example, substitutions may be made which more significantlyaffect: the structure of the polypeptide backbone in the area of thealteration, for example the alpha-helical or beta-sheet structure; thecharge or hydrophobicity of the molecule at the target site; or the bulkof the side chain. The substitutions which in general are expected toproduce the greatest changes in the polypeptide's properties are thosein which (a) a hydrophilic residue, e.g., serinyl or threonyl issubstituted for (or by) a hydrophobic residue, e.g., leucyl, isoleucyl,phenylalanyl, valyl or alanyl; (b) a cysteine or proline is substitutedfor (or by) another residue; (c) a residue having an electropositiveside chain, e.g., lysyl, arginyl, or histidyl, is substituted for (orby) an electronegative residue, e.g., glutamyl or aspartyl; or (d) aresidue having a bulky side chain, e.g., phenylalanine, is substitutedfor (or by) one not having a side chain, e.g., glycine.

Covalent modifications of prostate cancer polypeptides are includedwithin the scope of this invention. One type of covalent modificationincludes reacting targeted amino acid residues of a prostate cancerpolypeptide with an organic derivatizing agent that is capable ofreacting with selected side chains or the N- or C-terminal residues of aprostate cancer polypeptide. Derivatization with bifunctional agents isuseful, for instance, for crosslinking prostate cancer polypeptides to awater-insoluble support matrix or surface for use in the method forpurifying anti-prostate cancer polypeptide antibodies or screeningassays, as is more fully described below. Commonly used crosslinkingagents include, e.g., 1,1-bis(diazoacetyl)-2-phenylethane,glutaraldehyde, N-hydroxysuccinimide esters, e.g., esters with4-azidosalicylic acid, homobifunctional imidoesters, includingdisuccinimidyl esters such as 3,3′-dithiobis(succinimidylpropionate),bifunctional maleimides such as bis-N-maleimido-1,8-octane and agentssuch as methyl-3-((p-azidophenyl)dithio)propioimidate.

Other modifications include deamidation of glutaminyl and asparaginylresidues to the corresponding glutamyl and aspartyl residues,respectively, hydroxylation of proline and lysine, phosphorylation ofhydroxyl groups of serinyl, threonyl or tyrosyl residues, methylation ofthe amino groups of the lysine, arginine, and histidine side chains(e.g., pp. 79-86, Creighton (1983) Proteins: Structure and MolecularProperties Freeman), acetylation of the N-terminal amine, and amidationof a C-terminal carboxyl group.

Another type of covalent modification of the prostate cancer polypeptideincluded within the scope of this invention comprises altering thenative glycosylation pattern of the polypeptide. “Altering the nativeglycosylation pattern” is intended for purposes herein to mean deletingone or more carbohydrate moieties found in native sequence prostatecancer polypeptide, and/or adding one or more glycosylation sites thatare not present in the native sequence prostate cancer polypeptide.Glycosylation patterns can be altered in many ways. For example the useof different cell types to express prostate cancer-associated sequencescan result in different glycosylation patterns.

Addition of glycosylation sites to prostate cancer polypeptides may alsobe accomplished by altering the amino acid sequence thereof. Thealteration may be made, e.g., by the addition of, or substitution by,one or more serine or threonine residues to the native sequence prostatecancer polypeptide (for O-linked glycosylation sites). The prostatecancer amino acid sequence may optionally be altered through changes atthe DNA level, particularly by mutating the DNA encoding the prostatecancer polypeptide at preselected bases such that codons are generatedthat will translate into the desired amino acids.

Another means of increasing the number of carbohydrate moieties on theprostate cancer polypeptide is by chemical or enzymatic coupling ofglycosides to the polypeptide. Such methods are described in the art,e.g., in WO 87/05330, and pp. 259-306 in Aplin and Wriston (1981) CRCCrit. Rev. Biochem.

Removal of carbohydrate moieties present on the prostate cancerpolypeptide may be accomplished chemically or enzymatically or bymutational substitution of codons encoding for amino acid residues thatserve as targets for glycosylation. Chemical deglycosylation techniquesare known in the art and described, e.g., by Hakimuddin, et al. (1987)Arch. Biochem. Biophys. 259:52-57; and Edge, et al. (1981) Anal.Biochem. 118:131-137. Enzymatic cleavage of carbohydrate moieties onpolypeptides can be achieved by the use of a variety of endo- andexo-glycosidases as described by Thotakura, et al. (1987) Meth. Enzymol.138:350-359.

Another type of covalent modification of prostate cancer compriseslinking the prostate cancer polypeptide to one of a variety ofnonproteinaceous polymers, e.g., polyethylene glycol, polypropyleneglycol, or polyoxyalkylenes, in the manner set forth in U.S. Pat. Nos.4,640,835; 4,496,689; 4,301,144; 4,670,417; 4,791,192; or 4,179,337.

Prostate cancer polypeptides of the present invention may also bemodified in a way to form chimeric molecules comprising a prostatecancer polypeptide fused to another, heterologous polypeptide or aminoacid sequence. In one embodiment, such a chimeric molecule comprises afusion of a prostate cancer polypeptide with a tag polypeptide whichprovides an epitope to which an anti-tag antibody can selectively bind.The epitope tag is generally placed at the amino- or carboxyl-terminusof the prostate cancer polypeptide. The presence of such epitope-taggedforms of a prostate cancer polypeptide can be detected using an antibodyagainst the tag polypeptide. Also, provision of the epitope tag enablesthe prostate cancer polypeptide to be readily purified by affinitypurification using an anti-tag antibody or another type of affinitymatrix that binds to the epitope tag. In an alternative embodiment, thechimeric molecule may comprise a fusion of a prostate cancer polypeptidewith an immunoglobulin or a particular region of an immunoglobulin. Fora bivalent form of the chimeric molecule, such a fusion could be to theFc region of an IgG molecule.

Various tag polypeptides and their respective antibodies are well knownin the art. Examples include poly-histidine (poly-his) orpoly-histidine-glycine (poly-his-gly) tags; HIS6 and metal chelationtags, the flu HA tag polypeptide and its antibody 12CA5 (Field, et al.(1988) Mol. Cell. Biol. 8:2159-2165; the c-myc tag and the 8F9, 3C7,6E10, G4, B7, and 9E10 antibodies thereto (Evan, et al. (1985) Molecularand Cellular Biology 5:3610-3616); and the Herpes Simplex virusglycoprotein D (gD) tag and its antibody (Paborsky, et al. (1990)Protein Engineering 3:547-553). Other tag polypeptides include theFlag-peptide (Hopp, et al. (1988) BioTechnology 6:1204-1210); the KT3epitope peptide (Martin, et al. (1992) Science 255:192-194); tubulinepitope peptide (Skinner, et al. (1991) J. Biol. Chem. 266:15163-15166);and the T7 gene 10 protein peptide tag (Lutz-Freyermuth, et al. (1990)Proc. Natl. Acad. Sci. USA 87:6393-6397).

Also included are other prostate cancer proteins of the prostate cancerfamily, and prostate cancer proteins from other organisms, which arecloned and expressed as outlined below. Thus, probe or degeneratepolymerase chain reaction (PCR) primer sequences may be used to findother related prostate cancer proteins from humans or other organisms.As will be appreciated by those in the art, particularly useful probeand/or PCR primer sequences include the unique areas of the prostatecancer nucleic acid sequence. As is generally known in the art,preferred PCR primers are from about 15 to about 35 nucleotides inlength, with from about 20 to about 30 being preferred, and may containinosine as needed. The conditions for the PCR reaction are well known inthe art (e.g., Innis, PCR Protocols, supra).

Antibodies to Prostate Cancer Proteins

In a preferred embodiment, when the prostate cancer protein is to beused to generate antibodies, e.g., for immunotherapy or immunodiagnosis,the prostate cancer protein should share at least one epitope ordeterminant with the full length protein. By “epitope” or “determinant”herein is typically meant a portion of a protein which will generateand/or bind an antibody or T-cell receptor in the context of MHC. Thus,in most instances, antibodies made to a smaller prostate cancer proteinwill be able to bind to the full-length protein, particularly linearepitopes. In a preferred embodiment, the epitope is unique; that is,antibodies generated to a unique epitope show little or nocross-reactivity.

Methods of preparing polyclonal antibodies are known to the skilledartisan (e.g., Coligan, supra; and Harlow and Lane, supra). Polyclonalantibodies can be raised in a mammal, e.g., by one or more injections ofan immunizing agent and, if desired, an adjuvant. Typically, theimmunizing agent and/or adjuvant will be injected in the mammal bymultiple subcutaneous or intraperitoneal injections. The immunizingagent may include a protein encoded by a nucleic acid of the figures orfragment thereof or a fusion protein thereof. It may be useful toconjugate the immunizing agent to a protein known to be immunogenic inthe mammal being immunized. Examples of such immunogenic proteinsinclude but are not limited to keyhole limpet hemocyanin, serum albumin,bovine-thyroglobulin, and soybean trypsin inhibitor. Examples ofadjuvants which may be employed include Freund's complete adjuvant andMPL-TDM adjuvant (monophosphoryl Lipid A, synthetic trehalosedicorynomycolate). The immunization protocol may be selected by oneskilled in the art without undue experimentation.

The antibodies may, alternatively, be monoclonal antibodies. Monoclonalantibodies may be prepared using hybridoma methods, such as thosedescribed by Kohler and Milstein (1975) Nature 256:495. In a hybridomamethod, a mouse, hamster, or other appropriate host animal, is typicallyimmunized with an immunizing agent to elicit lymphocytes that produce orare capable of producing antibodies that will specifically bind to theimmunizing agent. Alternatively, the lymphocytes may be immunized invitro. The immunizing agent will typically include a polypeptide encodedby a nucleic acid of Tables 1A-4 or fragment thereof, or a fusionprotein thereof. Generally, either peripheral blood lymphocytes (“PBLs”)are used if cells of human origin are desired, or spleen cells or lymphnode cells are used if non-human mammalian sources are desired. Thelymphocytes are then fused with an immortalized cell line using asuitable fusing agent, such as polyethylene glycol, to form a hybridomacell (see pp. 59-103 in Goding (1986) Monoclonal Antibodies: Principlesand Practice Academic Press). Immortalized cell lines are usuallytransformed mammalian cells, particularly myeloma cells of rodent,bovine and human origin. Usually, rat or mouse myeloma cell lines areemployed. The hybridoma cells may be cultured in a suitable culturemedium that preferably contains one or more substances that inhibit thegrowth or survival of the unfused, immortalized cells. For example, ifthe parental cells lack the enzyme hypoxanthine guanine phosphoribosyltransferase (HGPRT or HPRT), the culture medium for the hybridomastypically will include hypoxanthine, aminopterin, and thymidine (“HATmedium”), which substances prevent the growth of HGPRT-deficient cells.

In one embodiment, the antibodies are bispecific antibodies. Bispecificantibodies are monoclonal, preferably human or humanized, antibodiesthat have binding specificities for at least two different antigens orthat have binding specificities for two epitopes on the same antigen. Inone embodiment, one of the binding specificities is for a proteinencoded by a nucleic acid of Tables 1A-4 or a fragment thereof, theother one is for another antigen, and preferably for a cell-surfaceprotein or receptor or receptor subunit, preferably one that is tumorspecific. Alternatively, tetramer-type technology may create multivalentreagents.

In a preferred embodiment, the antibodies to prostate cancer protein arecapable of reducing or eliminating a biological function of a prostatecancer protein, as is described below. That is, the addition ofanti-prostate cancer protein antibodies (either polyclonal or preferablymonoclonal) to prostate cancer tissue (or cells containing prostatecancer) may reduce or eliminate the prostate cancer. Generally, at leasta 25% decrease in activity, growth, size or the like is preferred, withat least about 50% being particularly preferred and about a 95-100%decrease being especially preferred.

In a preferred embodiment the antibodies to the prostate cancer proteinsare humanized antibodies (e.g., Xenerex Biosciences; Medarex, Inc.;Abgenix, Inc.; Protein Design Labs, Inc.). Humanized forms of non-human(e.g., murine) antibodies are chimeric molecules of immunoglobulins,immunoglobulin chains or fragments thereof (such as Fv, Fab, Fab′,F(ab′)2 or other antigen-binding subsequences of antibodies) whichcontain minimal sequence derived from non-human immunoglobulin.Humanized antibodies include human immunoglobulins (recipient antibody)in which residues from a complementary determining region (CDR) of therecipient are replaced by residues from a CDR of a non-human species(donor antibody) such as mouse, rat or rabbit having the desiredspecificity, affinity and capacity. In some instances, Fv frameworkresidues of the human immunoglobulin are replaced by correspondingnon-human residues. Humanized antibodies may also comprise residueswhich are found neither in the recipient antibody nor in the importedCDR or framework sequences. In general, a humanized antibody willcomprise substantially all of at least one, and typically two, variabledomains, in which all or substantially all of the CDR regions correspondto those of a non-human immunoglobulin and all or substantially all ofthe framework (FR) regions are those of a human immunoglobulin consensussequence. The humanized antibody optimally also will comprise at least aportion of an immunoglobulin constant region (Fc), typically that of ahuman immunoglobulin (Jones, et al. (1986) Nature 321:522-525;Riechmann, et al. (1988) Nature 332:323-329; and Presta (1992) Curr. Op.Struct. Biol. 2:593-596). Humanization can be essentially performedfollowing methods of Winter and co-workers (see, e.g., Jones, et al.(1986) Nature 321:522-525; Riechmann, et al. (1988) Nature 332:323-327;and Verhoeyen, et al. (1988) Science 239:1534-1536), by substitutingrodent CDRs or CDR sequences for the corresponding sequences of a humanantibody. Accordingly, such humanized antibodies are chimeric antibodies(U.S. Pat. No. 4,816,567), wherein substantially less than an intacthuman variable domain has been substituted by the corresponding sequencefrom a non-human species.

Human antibodies can also be produced using various techniques known inthe art, including phage display libraries (Hoogenboom and Winter (1991)J. Mol. Biol. 227:381-388; Marks, et al. (1991) J. Mol. Biol.222:581-597) or the preparation of human monoclonal antibodies (e.g., p77 in Cole, et al. (1985) Monoclonal Antibodies and Cancer Therapy Liss;and Boerner, et al. (1991) J. Immunol. 147(1):86-95). Similarly, humanantibodies can be made by introducing of human immunoglobulin loci intotransgenic animals, e.g., mice in which the endogenous immunoglobulingenes have been partially or completely inactivated. Upon challenge,human antibody production is observed, which closely resembles that seenin humans in most respects, including gene rearrangement, assembly, andantibody repertoire. This approach is described, e.g., in U.S. Pat. Nos.5,545,807; 5,545,806; 5,569,825; 5,625,126; 5,633,425; 5,661,016, and inthe following scientific publications: Marks, et al. (1992)Bio/Technology 10:779-783; Lonberg, et al. (1994) Nature 368:856-859;Morrison (1994) Nature 368:812-13; Fishwild, et al. (1996) NatureBiotechnology 14:845-51; Neuberger (1996) Nature Biotechnology 14:826;Lonberg and Huszar (1995) Intern. Rev. Immunol. 13:65-93.

By immunotherapy is meant treatment of prostate cancer with an antibodyraised against prostate cancer proteins. As used herein, immunotherapycan be passive or active. Passive immunotherapy as defined herein is thepassive transfer of antibody to a recipient (patient). Activeimmunization is the induction of antibody and/or T-cell responses in arecipient (patient). Induction of an immune response is the result ofproviding the recipient with an antigen to which antibodies are raised.As appreciated by one of ordinary skill in the art, the antigen may beprovided by injecting a polypeptide against which antibodies are desiredto be raised into a recipient, or contacting the recipient with anucleic acid capable of expressing the antigen and under conditions forexpression of the antigen, leading to an immune response.

In a preferred embodiment the prostate cancer proteins against whichantibodies are raised are secreted proteins as described above. Withoutbeing bound by theory, antibodies used for treatment, bind and preventthe secreted protein from binding to its receptor, thereby inactivatingthe secreted prostate cancer protein.

In another preferred embodiment, the prostate cancer protein to whichantibodies are raised is a transmembrane protein. Without being bound bytheory, antibodies used for treatment bind the extracellular domain ofthe prostate cancer protein and prevent it from binding to otherproteins, such as circulating ligands or cell-associated molecules. Theantibody may cause down-regulation of the transmembrane prostate cancerprotein. As will be appreciated by one of ordinary skill in the art, theantibody may be a competitive, non-competitive or uncompetitiveinhibitor of protein binding to the extracellular domain of the prostatecancer protein. The antibody is also often an antagonist of the prostatecancer protein. Further, the antibody may prevent activation of thetransmembrane prostate cancer protein. In one aspect, when the antibodyprevents the binding of other molecules to the prostate cancer protein,the antibody prevents growth of the cell. The antibody may also be usedto target or sensitize the cell to cytotoxic agents, including, but notlimited to TNF-α, TNF-β, IL-1, INF-γ, and IL-2, or chemotherapeuticagents including 5FU, vinblastine, actinomycin D, cisplatin,methotrexate, and the like. In some instances the antibody belongs to asub-type that activates serum complement when complexed with thetransmembrane protein thereby mediating cytotoxicity orantigen-dependent cytotoxicity (ADCC). Thus, prostate cancer is treatedby administering to a patient antibodies directed against thetransmembrane prostate cancer protein. Antibody-labeling may activate aco-toxin, localized toxin payload, or otherwise provide means to locallyablate cells.

In another preferred embodiment, the antibody is conjugated to aneffector moiety. The effector moiety can be a labeling moiety such as aradioactive label or fluorescent label, or can be a therapeutic moiety.In one aspect the therapeutic moiety is a small molecule that modulatesthe activity of the prostate cancer protein. In another aspect thetherapeutic moiety modulates the activity of molecules associated withor in close proximity to the prostate cancer protein. The therapeuticmoiety may inhibit enzymatic activity such as protease or collagenase orprotein kinase activity associated with prostate cancer.

In a preferred embodiment, the therapeutic moiety can also be acytotoxic agent. In this method, targeting the cytotoxic agent toprostate cancer tissue or cells, results in a reduction in the number ofafflicted cells, thereby reducing symptoms associated with prostatecancer. Cytotoxic agents are numerous and varied and include, but arenot limited to, cytotoxic drugs or toxins or active fragments of suchtoxins. Suitable toxins and their corresponding fragments includediphtheria A chain, exotoxin A chain, ricin A chain, abrin A chain,curcin, crotin, phenomycin, enomycin, saporin, auristatin, and the like.Cytotoxic agents also include radiochemicals made by conjugatingradioisotopes to antibodies raised against prostate cancer proteins, orbinding of a radionuclide to a chelating agent that has been covalentlyattached to the antibody. Targeting the therapeutic moiety totransmembrane prostate cancer proteins not only serves to increase thelocal concentration of therapeutic moiety in the prostate cancerafflicted area, but also serves to reduce deleterious side effects,e.g., by binding to normal tissues, that may be associated with thetherapeutic moiety.

In another preferred embodiment, the prostate cancer protein againstwhich the antibodies are raised is an intracellular protein. In thiscase, the antibody may be conjugated to a protein which facilitatesentry into the cell. In one case, the antibody enters the cell byendocytosis. In another embodiment, a nucleic acid encoding the antibodyis administered to the individual or cell. Moreover, wherein theprostate cancer protein can be targeted within a cell, i.e., thenucleus, an antibody thereto contains a signal for that targetlocalization, i.e., a nuclear localization signal.

The prostate cancer antibodies of the invention specifically bind toprostate cancer proteins. By “specifically bind” herein is meant thatthe antibodies bind to the protein with a K_(d) of at least about 0.1mM, more usually at least about 1 μM, preferably at least about 0.1 μMor better, and most preferably, 0.01 μM or better. Selectivity ofbinding is also important.

Detection of Prostate Cancer Sequence for Diagnostic and TherapeuticApplications

In one aspect, the RNA expression levels of genes are determined fordifferent cellular states in the prostate cancer phenotype. Afterandrogen ablation therapy, cells that survive the therapy undergo aperiod of quiescence followed at sometime later by active cell division.As explained above, there are a variety of expression patternscharacteristic of the prostate cancer genes involved inandrogen-independent prostate cancer. Some genes are expressed early inthe time course following ablation therapy, then drop off in expression,and then express again with emergence of androgen-independence (hi-lo-hipattern in 1A). Other genes are expressed early in the time coursefollowing ablation therapy, then drop off in expression, and do notexpress again with emergence of androgen-independence (hi-lo-lo patternin Table 1A). Still other genes are not expressed early in the timecourse, but express only with emergence of androgen-independence(lo-lo-hi pattern in Table 1A). Other genes are not expressed early inthe time course, but then express as androgen is withdrawn and continueto express with emergence of androgen-independence (lo-hi-hi pattern inTable 1A). Finally, some genes are not expressed early in the timecourse, but then express as androgen is withdrawn and drop off againwith emergence of androgen-independence (lo-hi-lo pattern in Table 1A).Thus, the data suggest that different antigens are expressed inquiescent cells and actively dividing androgen-independent prostatecancer cells.

In another aspect, the RNA expression levels of genes are determined fordifferent cellular states in the prostate cancer phenotype. Afterandrogen ablation therapy, cells that survive the therapy undergo aperiod of quiescence followed at sometime later by active cell division.As explained above, there are a variety of expression patternscharacteristic of the prostate cancer genes involved inandrogen-independent prostate cancer. Some genes are expressed early inthe time course following ablation therapy, then drop off in expression,and then express again with emergence of androgen-independence(hi-lo-lo-hi pattern in Table 2A). Other genes are expressed early inthe time course following ablation therapy, then drop off in expression,and do not express again with emergence of androgen-independence(hi-lo-lo-lo and hi-hi-lo-lo pattern in Table 2A). Still other genes arenot expressed early in the time course, but express only with emergenceof androgen-independence (lo-lo-lo-hi pattern in Table 2A). Other genesare not expressed early in the time course, but then express as androgenis withdrawn and continue to express with emergence ofandrogen-independence (lo-lo-hi-hi pattern in Table 2A). Finally, somegenes are not expressed early in the time course, but then express asandrogen is withdrawn and drop off again with emergence ofandrogen-independence (lo-lo-hi-lo pattern in Table 2A). Thus, the datasuggest that different antigens are expressed in quiescent cells (duringandrogen withdrawal) and actively dividing androgen-independent prostatecancer cells.

Effective therapy to combat androgen-independent prostate cancerrequires that the timing of therapy coincide with expression of thetarget genes. Patients can be monitored for the expression of certaindiagnostic antigens that indicate the presence of quiescent cells orwhich indicate the transition to actively dividing androgen-independentprostate cancer cells. Thus, therapy to combat androgen-independentprostate cancer should begin at some time following androgen ablationtherapy, depending on the particular target. Typically the transitionfrom quiescence to actively dividing androgen-independent prostatecancer occurs between 6-24 months following androgen ablation therapy.Thus, preferred time periods for the therapies of the invention are asfollows:

Expression levels of genes in normal tissue (i.e., not undergoingprostate cancer) and in prostate cancer tissue (and in some cases, forvarying severities of prostate cancer that relate to prognosis, asoutlined below) or in non-malignant disease are evaluated to provideexpression profiles. An expression profile of a particular cell state orpoint of development is essentially a “fingerprint” of the state. Whiletwo states may have a particular gene similarly expressed, theevaluation of a number of genes simultaneously allows the generation ofa gene expression profile that is reflective of the state of the cell.By comparing expression profiles of cells in different states,information regarding which genes are important (including both up- anddown-regulation of genes) in each of these states is obtained. Then,diagnosis may be performed or confirmed to determine whether a tissuesample has the gene expression profile of normal or cancerous tissue.This will provide for molecular diagnosis of related conditions.

“Differential expression,” or grammatical equivalents as used herein,refers to qualitative or quantitative differences in the temporal and/orcellular gene expression patterns within and among cells and tissue.Thus, a differentially expressed gene can qualitatively have itsexpression altered, including an activation or inactivation, in, e.g.,normal versus prostate cancer tissue. Genes may be turned on or turnedoff in a particular state, relative to another state thus permittingcomparison of two or more states. A qualitatively regulated gene willexhibit an expression pattern within a state or cell type which isdetectable by standard techniques. Some genes will be expressed in onestate or cell type, but not in both. Alternatively, the difference inexpression may be quantitative, e.g., in that expression is increased ordecreased; i.e., gene expression is either upregulated, resulting in anincreased amount of transcript, or downregulated, resulting in adecreased amount of transcript. The degree to which expression differsneed only be large enough to quantify via standard characterizationtechniques as outlined below, such as by use of Affymetrix GeneChip™expression arrays, Lockhart (1996) Nature Biotechnology 14:1675-1680,hereby expressly incorporated by reference. Other techniques include,but are not limited to, quantitative reverse transcriptase PCR, northernanalysis and RNase protection. As outlined above, preferably the changein expression (i.e., upregulation or downregulation) is at least about50%, more preferably at least about 100%, more preferably at least about150%, more preferably at least about 200%, with from 300 to at least1000% being especially preferred.

Evaluation may be at the gene transcript, or the protein level. Theamount of gene expression may be monitored using nucleic acid probes tothe DNA or RNA equivalent of the gene transcript, and the quantificationof gene expression levels, or, alternatively, the final gene productitself (protein) can be monitored, e.g., with antibodies to the prostatecancer protein and standard immunoassays (ELISAs, etc.) or othertechniques, including mass spectroscopy assays, 2D gel electrophoresisassays, etc. Proteins corresponding to prostate cancer genes, i.e.,those identified as being important in a prostate cancer or diseasephenotype, can be evaluated in a prostate cancer diagnostic test.

In a preferred embodiment, gene expression monitoring is performedsimultaneously on a number of genes. Multiple protein expressionmonitoring can be performed as well. Similarly, these assays may beperformed on an individual basis as well.

In this embodiment, the prostate cancer nucleic acid probes are attachedto biochips as outlined herein for the detection and quantification ofprostate cancer sequences in a particular cell. The assays are furtherdescribed below in the example. PCR techniques can be used to providegreater sensitivity.

In a preferred embodiment nucleic acids encoding the prostate cancerprotein are detected. Although DNA or RNA encoding the prostate cancerprotein may be detected, of particular interest are methods wherein anmRNA encoding a prostate cancer protein is detected. Probes to detectmRNA can be a nucleotide/deoxynucleotide probe that is complementary toand hybridizes with the mRNA and includes, but is not limited to,oligonucleotides, cDNA, or RNA. Probes also should contain a detectablelabel, as defined herein. In one method the mRNA is detected afterimmobilizing the nucleic acid to be examined on a solid support such asnylon membranes and hybridizing the probe with the sample. Followingwashing to remove the non-specifically bound probe, the label isdetected. In another method detection of the mRNA is performed in situ(in situ hybridization or ISH). In this method permeabilized cells ortissue samples are contacted with a detectably labeled nucleic acidprobe for sufficient time to allow the probe to hybridize with thetarget mRNA. Following washing to remove the non-specifically boundprobe, the label is detected. For example a digoxygenin labeledriboprobe (RNA probe) that is complementary to the mRNA encoding aprostate cancer protein is detected by binding the digoxygenin with ananti-digoxygenin secondary antibody and developed with nitro bluetetrazolium and 5-bromo-4-chloro-3-indoyl phosphate.

In a preferred embodiment, various proteins from the three classes ofproteins as described herein (secreted, transmembrane, or intracellularproteins) are used in diagnostic assays. The prostate cancer proteins,antibodies, nucleic acids, modified proteins and cells containingprostate cancer sequences are used in diagnostic assays. Such mayevaluate tissues, e.g., immunohistochemistry, or evaluate body fluids,e.g., blood. The detection may be direct of cells, or indirect, e.g., ofproducts from cells. This can be performed on an individual gene orcorresponding polypeptide level. In a preferred embodiment, theexpression profiles are used, preferably in conjunction with highthroughput screening techniques to allow monitoring for expressionprofile genes and/or corresponding polypeptides.

As described and defined herein, prostate cancer proteins, includingintracellular, transmembrane, or secreted proteins, find use asprognostic or diagnostic markers of prostate cancer or other prostateconditions. Detection of these proteins in putative prostate cancertissue allows for detection, diagnosis, or prognosis of prostateproliferative disorders (malignant and non-malignant) including benignprostate hyperplasia (BPH) and cancer, and prostatitis. Diagnosis mayalso assist in selecting a therapeutic strategy, e.g., based onexpression profiles and/or comparison to archival samples. In oneembodiment, antibodies are used to detect prostate cancer proteins,directly or indirectly. A preferred method separates proteins from asample by electrophoresis on a gel (typically a denaturing and reducingprotein gel, but may be another type of gel, including isoelectricfocusing gels and the like). Following separation of proteins, theprostate cancer protein is detected, e.g., by immunoblotting withantibodies raised against the prostate cancer protein. Methods ofimmunoblotting are well known to those of ordinary skill in the art.

In another preferred method, antibodies to the prostate cancer proteinfind use in in situ imaging techniques, e.g., in histology and/or inimmunohistochemistry (e.g., Asai (ed. 1993) Methods in Cell Biology:Antibodies in Cell Biology (vol. 37) Academic Press. In this methodcells are contacted with from one to many antibodies to the prostatecancer protein(s). Following washing to remove non-specific antibodybinding, the presence of the antibody or antibodies is detected. In oneembodiment the antibody is detected by incubating with a secondaryantibody that contains a detectable label. In another method the primaryantibody to the prostate cancer protein(s) contains a detectable label,e.g., an enzyme marker that can act on a substrate. In another preferredembodiment each one of multiple primary antibodies contains a distinctand detectable label. This method finds particular use in simultaneousscreening for a plurality of prostate cancer proteins. As will beappreciated by one of ordinary skill in the art, many other histologicalimaging techniques are also provided by the invention.

In a preferred embodiment the label is detected in a fluorometer whichhas the ability to detect and distinguish emissions of differentwavelengths. In addition, a fluorescence activated cell sorter (FACS)can be used in the method.

In another preferred embodiment, antibodies find use in diagnosingprostate cancer from blood, serum, plasma, stool, and other samples.Such samples, therefore, are useful as samples to be probed or testedfor the presence of prostate cancer proteins, which may be diagnostic ofprostate conditions beyond cancer, e.g., BPH. Antibodies can be used todetect a prostate cancer protein by previously described immunoassaytechniques including ELISA, immunoblotting (western blotting),immunoprecipitation, BIACORE technology, and the like. Conversely, thepresence of antibodies may indicate an immune response against anendogenous prostate cancer protein.

In a preferred embodiment, in situ hybridization of labeled prostatecancer nucleic acid probes to tissue arrays is done. For example, arraysof tissue samples, including prostate cancer tissue and/or normaltissue, are made. In situ hybridization (see, e.g., Ausubel, supra) isthen performed. When comparing the fingerprints between an individualand a standard, the skilled artisan can make a diagnosis, a prognosis,or a prediction based on the findings. It is further understood that thegenes which indicate the diagnosis may differ from those which indicatethe prognosis and molecular profiling of the condition of the cells maylead to distinctions between responsive or refractory conditions or maybe predictive of outcomes.

In a preferred embodiment, the prostate cancer proteins, antibodies,nucleic acids, modified proteins, and cells containing prostate cancersequences are used in prognosis assays. As above, gene expressionprofiles can be generated that correlate to prostate cancer or otherprostate disorders, in terms of useful aspects of clinical condition,pathology, or other information which may be relevant to long termprognosis. Again, this may be done on either a protein or gene level,with the use of genes being preferred. Single or multiple genes may beuseful in various combinations. As above, prostate cancer probes may beattached to biochips for the detection and quantification of prostatecancer sequences in a tissue or patient. The assays proceed as outlinedabove for diagnosis. PCR method may provide more sensitive and accuratequantification.

Assays for Therapeutic Compounds

In a preferred embodiment members of the proteins, nucleic acids, andantibodies as described herein are used in drug screening assays. Theprostate cancer proteins, antibodies, nucleic acids, modified proteins,and cells containing prostate cancer sequences are used in drugscreening assays or by evaluating the effect of drug candidates on a“gene expression profile” or expression profile of polypeptides. In apreferred embodiment, the expression profiles are used, preferably inconjunction with high throughput screening techniques to allowmonitoring for expression profile genes after treatment with a candidateagent (e.g., Zlokarnik, et al. (1998) Science 279:84-88; Heid (1996)Genome Res. 6:986-94).

In a preferred embodiment, the prostate cancer proteins, antibodies,nucleic acids, modified proteins, and cells containing the native ormodified prostate cancer proteins are used in screening assays. That is,the present invention provides novel methods for screening forcompositions which modulate the prostate cancer phenotype or anidentified physiological function of a prostate cancer protein. Asabove, this can be done on an individual gene level or by evaluating theeffect of drug candidates on a “gene expression profile”. In a preferredembodiment, the expression profiles are used, preferably in conjunctionwith high throughput screening techniques to allow monitoring forexpression profile genes after treatment with a candidate agent, seeZlokarnik, supra.

Having identified the differentially expressed genes herein, a varietyof assays may be executed. In a preferred embodiment, assays may be runon an individual gene or protein level. That is, having identified aparticular gene as up regulated in prostate cancer, test compounds canbe screened for the ability to modulate gene expression or for bindingto the prostate cancer protein. “Modulation” thus includes both anincrease and a decrease in gene expression. The preferred amount ofmodulation will depend on the original change of the gene expression innormal versus tissue undergoing prostate cancer, with changes of atleast 10%, preferably 50%, more preferably 100-300%, and in someembodiments 300-1000% or greater. Thus, if a gene exhibits a 4-foldincrease in prostate cancer tissue compared to normal tissue, a decreaseof about four-fold is often desired; similarly, a 10-fold decrease inprostate cancer tissue compared to normal tissue often provides a targetvalue of a 10-fold increase in expression to be induced by the testcompound.

The amount of gene expression may be monitored using nucleic acid probesand the quantification of gene expression levels, or, alternatively, thegene product itself can be monitored, e.g., through the use ofantibodies to the prostate cancer protein and standard immunoassays.Proteomics and separation techniques may also allow quantification ofexpression.

In a preferred embodiment, gene expression or protein monitoring of anumber of entities, i.e., an expression profile, is monitoredsimultaneously. Such profiles will typically involve a plurality ofthose entities described herein.

In this embodiment, the prostate cancer nucleic acid probes are attachedto biochips as outlined herein for the detection and quantification ofprostate cancer sequences in a particular cell. Alternatively, PCR maybe used. Thus, a series, e.g., of microtiter plate, may be used withdispensed primers in desired wells. A PCR reaction can then be performedand analyzed for each well.

Expression monitoring can be performed to identify compounds that modifythe expression of one or more prostate cancer-associated sequences,e.g., a polynucleotide sequence set out in Tables 1A-4. Generally, in apreferred embodiment, a test modulator is added to the cells prior toanalysis. Moreover, screens are also provided to identify agents thatmodulate prostate cancer, modulate prostate cancer proteins, bind to aprostate cancer protein, or interfere with the binding of a prostatecancer protein and an antibody or other binding partner.

The term “test compound” or “drug candidate” or “modulator” orgrammatical equivalents as used herein describes a molecule, e.g.,protein, oligopeptide, small organic molecule, polysaccharide,polynucleotide, etc., to be tested for the capacity to directly orindirectly alter the prostate cancer phenotype or the expression of aprostate cancer sequence, e.g., a nucleic acid or protein sequence. Inpreferred embodiments, modulators alter expression profiles, orexpression profile nucleic acids or proteins provided herein. In oneembodiment, the modulator suppresses a prostate cancer phenotype, e.g.,to a normal or non-malignant tissue fingerprint. In another embodiment,a modulator induced a prostate cancer phenotype. Generally, a pluralityof assay mixtures are run in parallel with different agentconcentrations to obtain a differential response to the variousconcentrations. Typically, one of these concentrations serves as anegative control, i.e., at zero concentration or below the level ofdetection.

Drug candidates encompass numerous chemical classes, though typicallythey are organic molecules, preferably small organic compounds having amolecular weight of more than 100 and less than about 2,500 daltons.Preferred small molecules are less than 2000, or less than 1500, or lessthan 1000, or less than 500 D. Candidate agents comprise functionalgroups necessary for structural interaction with proteins, particularlyhydrogen bonding, and typically include at least an amine, carbonyl,hydroxyl or carboxyl group, preferably at least two of the functionalchemical groups. The candidate agents often comprise cyclical carbon orheterocyclic structures and/or aromatic or polyaromatic structuressubstituted with one or more of the above functional groups. Candidateagents are also found among biomolecules including peptides,saccharides, fatty acids, steroids, purines, pyrimidines, derivatives,structural analogs, or combinations thereof. Particularly preferred arepeptides.

In one aspect, a modulator will neutralize the effect of a prostatecancer protein. By “neutralize” is meant that activity of a protein isinhibited or blocked and the consequent effect on the cell.

In certain embodiments, combinatorial libraries of potential modulatorswill be screened for an ability to bind to a prostate cancer polypeptideor to modulate activity. Conventionally, new chemical entities withuseful properties are generated by identifying a chemical compound(called a “lead compound”) with some desirable property or activity,e.g., inhibiting activity, creating variants of the lead compound, andevaluating the property and activity of those variant compounds. Often,high throughput screening (HTS) methods are employed for such ananalysis.

In one preferred embodiment, high throughput screening methods involveproviding a library containing a large number of potential therapeuticcompounds (candidate compounds). Such “combinatorial chemical libraries”are then screened in one or more assays to identify those librarymembers (particular chemical species or subclasses) that display adesired characteristic activity. The compounds thus identified can serveas conventional “lead compounds” or can themselves be used as potentialor actual therapeutics.

A combinatorial chemical library is a collection of diverse chemicalcompounds generated by either chemical synthesis or biological synthesisby combining a number of chemical “building blocks” such as reagents.For example, a linear combinatorial chemical library, such as apolypeptide (e.g., mutein) library, is formed by combining a set ofchemical building blocks called amino acids in most every possible wayfor a given compound length (i.e., the number of amino acids in apolypeptide compound). Millions of chemical compounds can be synthesizedthrough such combinatorial mixing of chemical building blocks. Gallop,et al. (1994) J. Med. Chem. 37:1233-1251.

Preparation and screening of combinatorial chemical libraries is wellknown to those of skill in the art. Such combinatorial chemicallibraries include, but are not limited to, peptide libraries (see, e.g.,U.S. Pat. No. 5,010,175, Furka (1991) Pept. Prot. Res. 37:487-493,Houghton, et al. (1991) Nature, 354:84-88), peptoids (PCT Publication NoWO 91/19735), encoded peptides (PCT Publication WO 93/20242), randombio-oligomers (PCT Publication WO 92/00091), benzodiazepines (U.S. Pat.No. 5,288,514), diversomers such as hydantoins, benzodiazepines anddipeptides (Hobbs, et al. (1993) Proc. Nat. Acad. Sci. USA90:6909-6913), vinylogous polypeptides (Hagihara, et al. (1992) J. Amer.Chem. Soc. 114:6568-xxx), nonpeptidal peptidomimetics with aBeta-D-Glucose scaffolding (Hirschmann, et al. (1992) J. Amer. Chem.Soc. 114:9217-9218), analogous organic syntheses of small compoundlibraries (Chen, et al. (1994) J. Amer. Chem. Soc. 116:2661-xxx),oligocarbamates (Cho, et al. (1993) Science 261:1303-1305), and/orpeptidyl phosphonates (Campbell, et al. (1994) J. Org. Chem.59:658-xxx). See, generally, Gordon, et al. (1994) J. Med. Chem.37:1385-1401), nucleic acid libraries (see, e.g., Stratagene, Corp.),peptide nucleic acid libraries (see, e.g., U.S. Pat. No. 5,539,083),antibody libraries (see, e.g., Vaughn, et al. (1996) NatureBiotechnology 14:309-314, and PCT/US96/10287), carbohydrate libraries(see, e.g., Liang, et al. (1996) Science 274:1520-1522, and U.S. Pat.No. 5,593,853), and small organic molecule libraries (see, e.g.,benzodiazepines, Baum (1993) C&EN, January 18, page 33; isoprenoids,U.S. Pat. No. 5,569,588; thiazolidinones and metathiazanones, U.S. Pat.No. 5,549,974; pyrrolidines, U.S. Pat. Nos. 5,525,735 and 5,519,134;morpholino compounds, U.S. Pat. No. 5,506,337; benzodiazepines, U.S.Pat. No. 5,288,514; and the like).

Devices for the preparation of combinatorial libraries are commerciallyavailable (see, e.g., 357 MPS, 390 MPS, Advanced Chem Tech, LouisvilleKy., Symphony, Rainin, Woburn, Mass., 433A Applied Biosystems, FosterCity, Calif., 9050 Plus, Millipore, Bedford, Mass.).

A number of well known robotic systems have also been developed forsolution phase chemistries. These systems include automated workstationslike the automated synthesis apparatus developed by Takeda ChemicalIndustries, LTD. (Osaka, Japan) and many robotic systems utilizingrobotic arms (Zymate II, Zymark Corporation, Hopkinton, Mass.; Orca,Hewlett-Packard, Palo Alto, Calif.), which mimic the manual syntheticoperations performed by a chemist. Many of the above devices aresuitable for use with the present invention. The nature andimplementation of modifications to these devices (if any) so that theycan operate as discussed herein will be apparent to persons skilled inthe relevant art. In addition, numerous combinatorial libraries arethemselves commercially available (see, e.g., ComGenex, Princeton, N.J.,Asinex, Moscow, Ru, Tripos, Inc., St. Louis, Mo., ChemStar, Ltd, Moscow,RU, 3D Pharmaceuticals, Exton, Pa., Martek Biosciences, Columbia, Md.,etc.).

The assays to identify modulators are amenable to high throughputscreening. Preferred assays thus detect enhancement or inhibition ofprostate cancer gene transcription, inhibition or enhancement ofpolypeptide expression, and inhibition or enhancement of polypeptideactivity.

High throughput assays for the presence, absence, quantification, orother properties of particular nucleic acids or protein products arewell known to those of skill in the art. Similarly, binding assays andreporter gene assays are similarly well known. Thus, e.g., U.S. Pat. No.5,559,410 discloses high throughput screening methods for proteins, U.S.Pat. No. 5,585,639 discloses high throughput screening methods fornucleic acid binding (i.e., in arrays), while U.S. Pat. Nos. 5,576,220and 5,541,061 disclose high throughput methods of screening forligand/antibody binding.

In addition, high throughput screening systems are commerciallyavailable (see, e.g., Zymark Corp., Hopkinton, Mass.; Air TechnicalIndustries, Mentor, Ohio; Beckman Instruments, Inc. Fullerton, Calif.;Precision Systems, Inc., Natick, Mass., etc.). These systems typicallyautomate entire procedures, including sample and reagent pipetting,liquid dispensing, timed incubations, and final readings of themicroplate in detector(s) appropriate for the assay. These configurablesystems provide high throughput and rapid start up as well as a highdegree of flexibility and customization. The manufacturers of suchsystems provide detailed protocols for various high throughput systems.Thus, e.g., Zymark Corp. provides technical bulletins describingscreening systems for detecting the modulation of gene transcription,ligand binding, and the like.

In one embodiment, modulators are proteins, often naturally occurringproteins or fragments of naturally occurring proteins. Thus, e.g.,cellular extracts containing proteins, or random or directed digests ofproteinaceous cellular extracts, may be used. In this way libraries ofproteins may be made for screening in the methods of the invention.Particularly preferred in this embodiment are libraries of bacterial,fungal, viral, and mammalian proteins, with the latter being preferred,and human proteins being especially preferred. Particularly useful testcompound will be directed to the class of proteins to which the targetbelongs, e.g., substrates for enzymes or ligands and receptors.

In a preferred embodiment, modulators are peptides of from about 5 toabout 30 amino acids, with from about 5 to about 20 amino acids beingpreferred, and from about 7 to about 15 being particularly preferred.The peptides may be digests of naturally occurring proteins as isoutlined above, random peptides, or “biased” random peptides. By“randomized” or grammatical equivalents herein is meant that eachnucleic acid and peptide consists of essentially random nucleotides andamino acids, respectively. Since generally these random peptides (ornucleic acids, discussed below) are chemically synthesized, they maytypically incorporate any nucleotide or amino acid at any position. Thesynthetic process can be designed to generate randomized proteins ornucleic acids, to allow the formation of all or most of the possiblecombinations over the length of the sequence, thus forming a library ofrandomized candidate bioactive proteinaceous agents.

In one embodiment, the library is fully randomized, with no sequencepreferences or constants at any position. In a preferred embodiment, thelibrary is biased. That is, some positions within the sequence areeither held constant, or are selected from a limited number ofpossibilities. For example, in a preferred embodiment, the nucleotidesor amino acid residues are randomized within a defined class, e.g., ofhydrophobic amino acids, hydrophilic residues, sterically biased (eithersmall or large) residues, towards the creation of nucleic acid bindingdomains, the creation of cysteines, for cross-linking, prolines for SH-3domains, serines, threonines, tyrosines, or histidines forphosphorylation sites, etc., or to purines, etc.

Modulators of prostate cancer can also be nucleic acids, as definedabove.

As described above generally for proteins, nucleic acid modulatingagents may be naturally occurring nucleic acids, random nucleic acids,or “biased” random nucleic acids. For example, digests of prokaryotic oreukaryotic genomes may be used as is outlined above for proteins.

In a preferred embodiment, the candidate compounds are organic chemicalmoieties, a wide variety of which are available in the literature.

After the candidate agent has been added and the cells allowed toincubate for some period of time, the sample containing a targetsequence to be analyzed is added to the biochip. If required, the targetsequence is prepared using known techniques. For example, the sample maybe treated to lyse the cells, using known lysis buffers,electroporation, etc., with purification and/or amplification such asPCR performed as appropriate. For example, an in vitro transcriptionwith labels covalently attached to the nucleotides is performed.Generally, the nucleic acids are labeled with biotin-FITC or PE, or withcy3 or cy5.

In a preferred embodiment, the target sequence is labeled with, e.g., afluorescent, a chemiluminescent, a chemical, or a radioactive signal, toprovide a means of detecting the target sequence's specific binding to aprobe. The label also can be an enzyme, such as, alkaline phosphatase orhorseradish peroxidase, which when provided with an appropriatesubstrate produces a product that can be detected. Alternatively, thelabel can be a labeled compound or small molecule, such as an enzymeinhibitor, that binds but is not catalyzed or altered by the enzyme. Thelabel also can be a moiety or compound, such as, an epitope tag orbiotin which specifically binds to streptavidin. For the example ofbiotin, the streptavidin is labeled as described above, thereby,providing a detectable signal for the bound target sequence. Unboundlabeled streptavidin is typically removed prior to analysis.

As will be appreciated by those in the art, these assays can be directhybridization assays or can comprise “sandwich assays”, which includethe use of multiple probes, as is generally outlined in U.S. Pat. Nos.5,681,702, 5,597,909, 5,545,730, 5,594,117, 5,591,584, 5,571,670,5,580,731, 5,571,670, 5,591,584, 5,624,802, 5,635,352, 5,594,118,5,359,100, 5,124,246, and 5,681,697, each of which is herebyincorporated by reference. In this embodiment, in general, the targetnucleic acid is prepared as outlined above, and then added to thebiochip comprising a plurality of nucleic acid probes, under conditionsthat allow the formation of a hybridization complex.

A variety of hybridization conditions may be used in the presentinvention, including high, moderate, and low stringency conditions asoutlined above. The assays are generally run under stringency conditionswhich allows formation of the label probe hybridization complex only inthe presence of target. Stringency can be controlled by altering a stepparameter that is a thermodynamic variable, including, but not limitedto, temperature, formamide concentration, salt concentration, chaotropicsalt concentration pH, organic solvent concentration, etc.

These parameters may also be used to control non-specific binding, as isgenerally outlined in U.S. Pat. No. 5,681,697. Thus it may be desirableto perform certain steps at higher stringency conditions to reducenon-specific binding.

The reactions outlined herein may be accomplished in a variety of ways.Components of the reaction may be added simultaneously, or sequentially,in different orders, with preferred embodiments outlined below. Inaddition, the reaction may include a variety of other reagents. Theseinclude salts, buffers, neutral proteins, e.g., albumin, detergents,etc., which may be used to facilitate optimal hybridization anddetection, and/or reduce non-specific or background interactions.Reagents that otherwise improve the efficiency of the assay, such asprotease inhibitors, nuclease inhibitors, anti-microbial agents, etc.,may also be used as appropriate, depending on the sample preparationmethods and purity of the target.

The assay data are analyzed to determine the expression levels, andchanges in expression levels as between states, of individual genes,forming a gene expression profile.

Screens are performed to identify modulators of the prostate cancer orrelated phenotype. In one embodiment, screening is performed to identifymodulators that can induce or suppress a particular expression profile,thus preferably generating the associated phenotype. In anotherembodiment, e.g., for diagnostic applications, having identifieddifferentially expressed genes important in a particular state, screenscan be performed to identify modulators that alter expression ofindividual genes. In an another embodiment, screening is performed toidentify modulators that alter a biological function of the expressionproduct of a differentially expressed gene. Again, having identified theimportance of a gene in a particular state, screens are performed toidentify agents that bind and/or modulate the biological activity of thegene product.

In addition screens can be done for genes that are induced in responseto a candidate agent. After identifying a modulator based upon itsability to suppress a prostate cancer expression pattern leading to anormal expression pattern, or to modulate a single prostate cancer geneexpression profile so as to mimic the expression of the gene from normaltissue, a screen as described above can be performed to identify genesthat are specifically modulated in response to the agent. Comparingexpression profiles between normal tissue and agent treated prostatecancer tissue reveals genes that are not expressed in normal tissue orprostate cancer tissue, but are expressed in agent treated tissue. Theseagent-specific sequences can be identified and used by methods describedherein for prostate cancer genes or proteins. In particular thesesequences and the proteins they encode find use in marking oridentifying agent treated cells. In addition, antibodies can be raisedagainst the agent induced proteins and used to target novel therapeuticsto the treated prostate cancer tissue sample.

Thus, in one embodiment, a test compound is administered to a populationof prostate cancer cells, that have an associated prostate cancerexpression profile. By “administration” or “contacting” herein is meantthat the candidate agent is added to the cells in such a manner as toallow the agent to act upon the cell, whether by uptake andintracellular action, or by action at the cell surface. In someembodiments, nucleic acid encoding a proteinaceous candidate agent(e.g., a peptide) may be put into a viral construct such as anadenoviral or retroviral construct, and added to the cell, such thatexpression of the peptide agent is accomplished, e.g., PCT US97/01019.Regulatable gene therapy systems can also be used.

Once the test compound has been administered to the cells, the cells canbe washed if desired and are allowed to incubate under preferablyphysiological conditions for some period of time. The cells are thenharvested and a new gene expression profile is generated, as outlinedherein.

Thus, e.g., prostate cancer or non-malignant tissue may be screened foragents that modulate, e.g., induce or suppress the prostate cancer orrelated phenotype. A change in at least one gene, preferably many, ofthe expression profile indicates that the agent has an effect onprostate cancer activity. By defining such a signature for the prostatecancer phenotype, screens for new drugs that alter the phenotype can bedevised. With this approach, the drug target need not be known and neednot be represented in the original expression screening platform, nordoes the level of transcript for the target protein need to change.

In a preferred embodiment, as outlined above, screens may be done onindividual genes and gene products (proteins). That is, havingidentified a particular differentially expressed gene as important in aparticular state, screening of modulators of either the expression ofthe gene or the gene product itself can be done. The gene products ofdifferentially expressed genes are sometimes referred to herein as“prostate cancer proteins” or a “prostate cancer modulatory protein”.The prostate cancer modulatory protein may be a fragment, oralternatively, be the full length protein to the fragment encoded by thenucleic acids of the Tables 1A-4. Preferably, the prostate cancermodulatory protein is a fragment. In a preferred embodiment, theprostate cancer amino acid sequence which is used to determine sequenceidentity or similarity is encoded by a nucleic acid of Tables 1A-4. Inanother embodiment, the sequences are naturally occurring allelicvariants of a protein encoded by a nucleic acid of Tables 1A-4. Inanother embodiment, the sequences are sequence variants as furtherdescribed herein.

Preferably, the prostate cancer modulatory protein is a fragment ofapproximately 14 to 24 amino acids long. More preferably the fragment isa soluble fragment. Preferably, the fragment includes anon-transmembrane region. In a preferred embodiment, the fragment has anN-terminal Cys to aid in solubility. In one embodiment, the C-terminusof the fragment is kept as a free acid and the N-terminus is a freeamine to aid in coupling, i.e., to cysteine.

In one embodiment the prostate cancer proteins are conjugated to animmunogenic agent as discussed herein. In one embodiment the prostatecancer protein is conjugated to BSA.

Measurements of prostate cancer polypeptide activity, or of prostatecancer or the prostate cancer phenotype can be performed using a varietyof assays. For example, the effects of the test compounds upon thefunction of the prostate cancer polypeptides can be measured byexamining parameters described above. A suitable physiological changethat affects activity can be used to assess the influence of a testcompound on the polypeptides of this invention. When the functionalconsequences are determined using intact cells or animals, one can alsomeasure a variety of effects such as, in the case of prostate cancerassociated with tumors, tumor growth, tumor metastasis,neovascularization, hormone release, transcriptional changes to bothknown and uncharacterized genetic markers (e.g., northern blots),changes in cell metabolism such as cell growth or pH changes, andchanges in intracellular second messengers such as cGMP. In the assaysof the invention, a mammalian prostate cancer polypeptide is typicallyused, e.g., mouse, preferably human.

Assays to identify compounds with modulating activity can be performedin vitro. For example, a prostate cancer polypeptide is first contactedwith a potential modulator and incubated for a suitable amount of time,e.g., from 0.5 to 48 hours. In one embodiment, the prostate cancerpolypeptide levels are determined in vitro by measuring the level ofprotein or mRNA. The level of protein is measured using immunoassayssuch as western blotting, ELISA, and the like with an antibody thatselectively binds to the prostate cancer polypeptide or a fragmentthereof. For measurement of mRNA, amplification, e.g., using PCR, LCR,or hybridization assays, e.g., northern hybridization, RNAse protection,dot blotting, are preferred. The level of protein or mRNA is detectedusing directly or indirectly labeled detection agents, e.g.,fluorescently or radioactively labeled nucleic acids, radioactively orenzymatically labeled antibodies, and the like, as described herein.

Alternatively, a reporter gene system can be devised using the prostatecancer protein promoter operably linked to a reporter gene such asluciferase, green fluorescent protein, CAT, or β-gal. The reporterconstruct is typically transfected into a cell. After treatment with apotential modulator, the amount of reporter gene transcription,translation, or activity is measured according to standard techniquesknown to those of skill in the art.

In a preferred embodiment, as outlined above, screens may be done onindividual genes and gene products (proteins). That is, havingidentified a particular differentially expressed gene as important in aparticular state, screening of modulators of the expression of the geneor the gene product itself can be done. The gene products ofdifferentially expressed genes are sometimes referred to herein as“prostate cancer proteins.” The prostate cancer protein may be afragment, or alternatively, be the full length protein corresponding toa fragment shown herein.

In one embodiment, screening for modulators of expression of specificgenes is performed. Typically, the expression of only one or a few genesare evaluated. In another embodiment, screens are designed to first findcompounds that bind to differentially expressed proteins. Thesecompounds are then evaluated for the ability to modulate differentiallyexpressed activity. Moreover, once initial candidate compounds areidentified, variants can be further screened to better evaluatestructure activity relationships.

In a preferred embodiment, binding assays are done. In general, purifiedor isolated gene product is used; that is, the gene products of one ormore differentially expressed nucleic acids are made. For example,antibodies are generated to the protein gene products, and standardimmunoassays are run to determine the amount of protein present.Alternatively, cells comprising the prostate cancer proteins can be usedin the assays.

Thus, in a preferred embodiment, the methods comprise combining aprostate cancer protein and a candidate compound, and determining thebinding of the compound to the prostate cancer protein. Preferredembodiments utilize the human prostate cancer protein, although othermammalian proteins may also be used, e.g., for the development of animalmodels of human disease. In some embodiments, as outlined herein,variant or derivative prostate cancer proteins may be used.

Generally, in a preferred embodiment of the methods herein, the prostatecancer protein or the candidate agent is non-diffusably bound to aninsoluble support having isolated sample receiving areas (e.g., amicrotiter plate, an array, etc.). The insoluble supports may be made ofa composition to which the compositions can be bound, is readilyseparated from soluble material, and is otherwise compatible with theoverall method of screening. The surface of such supports may be solidor porous and of a convenient shape. Examples of suitable insolublesupports include microtiter plates, arrays, membranes, and beads. Theseare typically made of glass, plastic (e.g., polystyrene),polysaccharides, nylon or nitrocellulose, teflon™, etc. Microtiterplates and arrays are especially convenient because a large number ofassays can be carried out simultaneously, using small amounts ofreagents and samples. The particular manner of binding of thecomposition should be compatible with the reagents and overall methodsof the invention, maintain the activity of the composition, and benondiffusable. Preferred methods of binding include the use ofantibodies (which do not sterically block either the ligand binding siteor activation sequence when the protein is bound to the support), directbinding to “sticky” or ionic supports, chemical crosslinking, thesynthesis of the protein or agent on the surface, etc. Following bindingof the protein or agent, excess unbound material is removed by washing.The sample receiving areas may then be blocked through incubation withbovine serum albumin (BSA), casein, or other innocuous protein or othermoiety.

In a preferred embodiment, the prostate cancer protein is bound to thesupport, and a test compound is added to the assay. Alternatively, thecandidate agent is bound to the support and the prostate cancer proteinis added. Novel binding agents include specific antibodies, non-naturalbinding agents identified in screens of chemical libraries, peptideanalogs, etc. Of particular interest are screening assays for agentsthat have a low toxicity for human cells. A wide variety of assays maybe used for this purpose, including labeled in vitro protein-proteinbinding assays, electrophoretic mobility shift assays, immunoassays forprotein binding, functional assays (phosphorylation assays, etc.) andthe like.

The determination of the binding of the test modulating compound to theprostate cancer protein may be done in a number of ways. In a preferredembodiment, the compound is labeled, and binding determined directly,e.g., by attaching all or a portion of the prostate cancer protein to asolid support, adding a labeled candidate agent (e.g., a fluorescentlabel), washing off excess reagent, and determining whether the label ispresent on the solid support. Various blocking and washing steps may beutilized as appropriate.

In some embodiments, only one of the components is labeled, e.g., theproteins (or proteinaceous candidate compounds) can be labeled.Alternatively, more than one component can be labeled with differentlabels, e.g., ¹²⁵I for the proteins and a fluorophor for the compound.Proximity reagents, e.g., quenching or energy transfer reagents are alsouseful.

In one embodiment, the binding of the test compound is determined bycompetitive binding assay. The competitor is a binding moiety known tobind to the target molecule (i.e., a prostate cancer protein), such asan antibody, peptide, binding partner, ligand, etc. Under certaincircumstances, there may be competitive binding between the compound andthe binding moiety, with the binding moiety displacing the compound. Inone embodiment, the test compound is labeled. Either the compound, orthe competitor, or both, is added first to the protein for a timesufficient to allow binding, if present. Incubations may be performed ata temperature which facilitates optimal activity, typically between 4and 40° C. Incubation periods are typically optimized, e.g., tofacilitate rapid high throughput screening. Typically between 0.1 and 1hour will be sufficient. Excess reagent is generally removed or washedaway. The second component is then added, and the presence or absence ofthe labeled component is followed, to indicate binding.

In a preferred embodiment, the competitor is added first, followed bythe test compound. Displacement of the competitor is an indication thatthe test compound is binding to the prostate cancer protein and thus iscapable of binding to, and potentially modulating, the activity of theprostate cancer protein. In this embodiment, either component can belabeled. Thus, e.g., if the competitor is labeled, the presence of labelin the wash solution indicates displacement by the agent. Alternatively,if the test compound is labeled, the presence of the label on thesupport indicates displacement.

In an alternative embodiment, the test compound is added first, withincubation and washing, followed by the competitor. The absence ofbinding by the competitor may indicate that the test compound is boundto the prostate cancer protein with a higher affinity. Thus, if the testcompound is labeled, the presence of the label on the support, coupledwith a lack of competitor binding, may indicate that the test compoundis capable of binding to the prostate cancer protein.

In a preferred embodiment, the methods comprise differential screeningto identity agents that are capable of modulating the activity of theprostate cancer proteins. In this embodiment, the methods comprisecombining a prostate cancer protein and a competitor in a first sample.A second sample comprises a test compound, a prostate cancer protein,and a competitor. The binding of the competitor is determined for bothsamples, and a change, or difference in binding between the two samplesindicates the presence of an agent capable of binding to the prostatecancer protein and potentially modulating its activity. That is, if thebinding of the competitor is different in the second sample relative tothe first sample, the agent is capable of binding to the prostate cancerprotein.

Alternatively, differential screening is used to identify drugcandidates that bind to the native prostate cancer protein, but cannotbind to modified prostate cancer proteins. The structure of the prostatecancer protein may be modeled, and used in rational drug design tosynthesize agents that interact with that site. Drug candidates thataffect the activity of a prostate cancer protein are also identified byscreening drugs for the ability to either enhance or reduce the activityof the protein.

Positive controls and negative controls may be used in the assays.Preferably control and test samples are performed in at least triplicateto obtain statistically significant results. Incubation of samples isfor a time sufficient for the binding of the agent to the protein.Following incubation, samples are washed free of non-specifically boundmaterial and the amount of bound, generally labeled agent determined.For example, where a radiolabel is employed, the samples may be countedin a scintillation counter to determine the amount of bound compound.

A variety of other reagents may be included in the screening assays.These include reagents like salts, neutral proteins, e.g., albumin,detergents, etc., which may be used to facilitate optimalprotein-protein binding and/or reduce non-specific or backgroundinteractions. Also reagents that otherwise improve the efficiency of theassay, such as protease inhibitors, nuclease inhibitors, anti-microbialagents, etc., may be used. The mixture of components may be added in anorder that provides for the requisite binding.

In a preferred embodiment, the invention provides methods for screeningfor a compound capable of modulating the activity of a prostate cancerprotein. The methods comprise adding a test compound, as defined above,to a cell comprising prostate cancer proteins. Preferred cell typesinclude almost any cell. The cells contain a recombinant nucleic acidthat encodes a prostate cancer protein. In a preferred embodiment, alibrary of candidate agents are tested on a plurality of cells.

In one aspect, the assays are evaluated in the presence or absence orprevious or subsequent exposure of physiological signals, e.g.,hormones, antibodies, peptides, antigens, cytokines, growth factors,action potentials, pharmacological agents including chemotherapeutics,radiation, carcinogenics, or other cells (e.g., cell-cell contacts). Inanother example, the determinations are determined at different stagesof the cell cycle process.

In this way, compounds that modulate prostate cancer agents areidentified. Compounds with pharmacological activity are able to enhanceor interfere with the activity of the prostate cancer protein. Onceidentified, similar structures are evaluated to identify criticalstructural feature of the compound.

In one embodiment, a method of inhibiting prostate cancer cell divisionis provided. The method comprises administration of a prostate cancerinhibitor. In another embodiment, a method of inhibiting prostate canceror other prostate proliferative condition is provided. The methodcomprises administration of a prostate cancer inhibitor. In a furtherembodiment, methods of treating cells or individuals with prostatecancer are provided. The method comprises administration of a prostatecancer inhibitor.

In one embodiment, a prostate cancer inhibitor is an antibody asdiscussed above. In another embodiment, the prostate cancer inhibitor isan antisense molecule.

A variety of cell growth, proliferation, and metastasis assays are knownto those of skill in the art, as described below.

Soft Agar Growth or Colony Formation in Suspension

Normal cells require a solid substrate to attach and grow. When thecells are transformed, they lose this phenotype and grow detached fromthe substrate. For example, transformed cells can grow in stirredsuspension culture or suspended in semi-solid media, such as semi-solidor soft agar. The transformed cells, when transfected with tumorsuppressor genes, regenerate normal phenotype and require a solidsubstrate to attach and grow. Soft agar growth or colony formation insuspension assays can be used to identify modulators of prostate cancersequences, which when expressed in host cells, inhibit abnormal cellularproliferation and transformation. A therapeutic compound would reduce oreliminate the host cells' ability to grow in stirred suspension cultureor suspended in semi-solid media, such as semi-solid or soft.

Techniques for soft agar growth or colony formation in suspension assaysare described in Freshney (1994) Culture of Animal Cells a Manual ofBasic Technique 3d ed. Wiley-Liss, herein incorporated by reference. Seealso, the methods section of Garkavtsev, et al. (1996), supra, hereinincorporated by reference.

Contact Inhibition and Density Limitation of Growth

Normal cells typically grow in a flat and organized pattern in a petridish until they touch other cells. When the cells touch one another,they are contact inhibited and stop growing. When cells are transformed,however, the cells are not contact inhibited and continue to grow tohigh densities in disorganized foci. Thus, the transformed cells grow toa higher saturation density than normal cells. This can be detectedmorphologically by the formation of a disoriented monolayer of cells orrounded cells in foci within the regular pattern of normal surroundingcells. Alternatively, labeling index with (³H)-thymidine at saturationdensity can be used to measure density limitation of growth. SeeFreshney (1994), supra. The transformed cells, when transfected withtumor suppressor genes, regenerate a normal phenotype and become contactinhibited and would grow to a lower density.

In this assay, labeling index with (³H)-thymidine at saturation densityis a preferred method of measuring density limitation of growth.Transformed host cells are transfected with a prostate cancer-associatedsequence and are grown for 24 hours at saturation density innon-limiting medium conditions. The percentage of cells labeling with(3H)-thymidine is determined autoradiographically. See, Freshney (1994),supra.

Growth Factor or Serum Dependence

Transformed cells have a lower serum dependence than their normalcounterparts (see, e.g., Temin (1966) J. Natl. Cancer Insti. 37:167-175;Eagle, et al. (1970) J. Exp. Med. 131:836-879); Freshney, supra. This isin part due to release of various growth factors by the transformedcells. Growth factor or serum dependence of transformed host cells canbe compared with that of control.

Tumor Specific Markers Levels

Tumor cells release an increased amount of certain factors (hereinafter“tumor specific markers”) than their normal counterparts. For example,plasminogen activator (PA) is released from human glioma at a higherlevel than from normal brain cells (see, e.g., Gullino, “Angiogenesis,tumor vascularization, and potential interference with tumor growth” pp.178-184 in Mihich (ed. 1985) Biological Responses in Cancer Plenum.Similarly, Tumor angiogenesis factor (TAF) is released at a higher levelin tumor cells than their normal counterparts. See, e.g., Folkman (1992)Angiogenesis and Cancer, Sem. Cancer Biol.

Various techniques which measure the release of these factors aredescribed in Freshney (1994), supra. Also, see, Unkless, et al. (1974)J. Biol. Chem. 249:4295-4305; Strickland and Beers (1976) J. Biol. Chem.251:5694-5702; Whur, et al. (1980) Br. J. Cancer 42:305-312; Gullino,“Angiogenesis, tumor vascularization, and potential interference withtumor growth” pp. 178-184 in Mihich (ed. 1985) Biological Responses inCancer Plenum; and Freshney (1985) Anticancer Res. 5:111-130.

Invasiveness into Matrigel

The degree of invasiveness into Matrigel or some other extracellularmatrix constituent can be used as an assay to identify compounds thatmodulate prostate cancer-associated sequences. Tumor cells exhibit agood correlation between malignancy and invasiveness of cells intoMatrigel or some other extracellular matrix constituent. In this assay,tumorigenic cells are typically used as host cells. Expression of atumor suppressor gene in these host cells would decrease invasiveness ofthe host cells.

Techniques described in Freshney (1994), supra, can be used. Briefly,the level of invasion of host cells can be measured by using filterscoated with Matrigel or some other extracellular matrix constituent.Penetration into the gel, or through to the distal side of the filter,is rated as invasiveness, and rated histologically by number of cellsand distance moved, or by prelabeling the cells with ¹²⁵I and countingthe radioactivity on the distal side of the filter or bottom of thedish. See, e.g., Freshney (1984), supra.

Tumor Growth In Vivo

Effects of prostate cancer-associated sequences on cell growth can betested in transgenic or immune-suppressed mice. Knock-out transgenicmice can be made, in which the prostate cancer gene is disrupted or inwhich a prostate cancer gene is inserted. Knock-out transgenic mice canbe made by insertion of a marker gene or other heterologous gene intothe endogenous prostate cancer gene site in the mouse genome viahomologous recombination. Such mice can also be made by substituting theendogenous prostate cancer gene with a mutated version of the prostatecancer gene, or by mutating the endogenous prostate cancer gene, e.g.,by exposure to carcinogens.

A DNA construct is introduced into the nuclei of embryonic stem cells.Cells containing the newly engineered genetic lesion are injected into ahost mouse embryo, which is re-implanted into a recipient female. Someof these embryos develop into chimeric mice that possess germ cellspartially derived from the mutant cell line. Therefore, by breeding thechimeric mice it is possible to obtain a new line of mice containing theintroduced genetic lesion (see, e.g., Capecchi, et al. (1989) Science244:1288-1292). Chimeric targeted mice can be derived according toHogan, et al. (1988) Manipulating the Mouse Embryo: A Laboratory ManualCSH Press; and Robertson (ed. 1987) Teratocarcinomas and Embryonic StemCells: A Practical Approach IRL Press, Washington, D.C.

Alternatively, various immune-suppressed or immune-deficient hostanimals can be used. For example, genetically athymic “nude” mouse (see,e.g., Giovanella, et al. (1974) J. Natl. Cancer Inst. 52:921-930), aSCID mouse, a thymectomized mouse, or an irradiated mouse (see, e.g.,Bradley, et al. (1978) Br. J. Cancer 38:263-272; Selby, et al. (1980)Br. J. Cancer 41:52-61) can be used as a host. Transplantable tumorcells (typically about 10⁶ cells) injected into isogenic hosts willproduce invasive tumors in a high proportions of cases, while normalcells of similar origin will not. In hosts which developed invasivetumors, cells expressing a prostate cancer-associated sequences areinjected subcutaneously. After a suitable length of time, preferably 4-8weeks, tumor growth is measured (e.g., by volume or by its two largestdimensions) and compared to the control. Tumors that have statisticallysignificant reduction (using, e.g., Student's T test) are said to haveinhibited growth.

Polynucleotide Modulators of Prostate Cancer

Antisense and RNAi Polynucleotides

In certain embodiments, the activity of a prostate cancer-associatedprotein is down-regulated, or entirely inhibited, by the use ofantisense polynucleotide, i.e., a nucleic acid complementary to, andwhich can preferably hybridize specifically to, a coding mRNA nucleicacid sequence, e.g., a prostate cancer protein mRNA, or a subsequencethereof. Binding of the antisense polynucleotide to the mRNA reduces thetranslation and/or stability of the mRNA.

In the context of this invention, antisense polynucleotides can comprisenaturally-occurring nucleotides, or synthetic species formed fromnaturally-occurring subunits or their close homologs. Antisensepolynucleotides may also have altered sugar moieties or inter-sugarlinkages. Exemplary among these are the phosphorothioate and othersulfur containing species which are known for use in the art. Analogsare comprehended by this invention so long as they function effectivelyto hybridize with the prostate cancer protein mRNA. See, e.g., IsisPharmaceuticals, Carlsbad, Calif.; Sequitor, Inc., Natick, Mass.

Such antisense polynucleotides can readily be synthesized usingrecombinant means, or can be synthesized in vitro. Equipment for suchsynthesis is sold by several vendors, including Applied Biosystems. Thepreparation of other oligonucleotides such as phosphorothioates andalkylated derivatives is also well known to those of skill in the art.

Antisense molecules as used herein include antisense or senseoligonucleotides. Sense oligonucleotides can, e.g., be employed to blocktranscription by binding to the anti-sense strand. The antisense andsense oligonucleotide comprise a single-stranded nucleic acid sequence(either RNA or DNA) capable of binding to target mRNA (sense) or DNA(antisense) sequences for prostate cancer molecules. A preferredantisense molecule is for a prostate cancer sequences in Tables 1A-4, orfor a ligand or activator thereof. Antisense or sense oligonucleotides,according to the present invention, comprise a fragment generally atleast about 14 nucleotides, preferably from about 14 to 30 nucleotides.The ability to derive an antisense or a sense oligonucleotide, basedupon a cDNA sequence encoding a given protein is described in, e.g.,Stein and Cohen (1988) Cancer Res. 48:2659-2668; and van der Krol, etal. (1988) BioTechniques 6:958-976.

RNA interference is a mechanism to suppress gene expression in asequence specific manner. See, e.g., Brumelkamp, et al. (2002)Sciencexpress (21Mar. 2002); Sharp (1999) Genes Dev. 13:139-141; andCathew (2001) Curr. Op. Cell Biol. 13:244-248. In mammalian cells,short, e.g., 21 nt, double stranded small interfering RNAs (siRNA) havebeen shown to be effective at inducing an RNAi response. See, e.g.,Elbashir, et al. (2001) Nature 411:494-498. The mechanism may be used todownregulate expression levels of identified genes, e.g., treatment ofor validation of relevance to disease.

Ribozymes

In addition to antisense polynucleotides, ribozymes can be used totarget and inhibit transcription of prostate cancer-associatednucleotide sequences. A ribozyme is an RNA molecule that catalyticallycleaves other RNA molecules. Different kinds of ribozymes have beendescribed, including group I ribozymes, hammerhead ribozymes, hairpinribozymes, RNase P, and axhead ribozymes (see, e.g., Castanotto, et al.(1994) Adv. in Pharmacology 25: 289-317 for a general review of theproperties of different ribozymes).

The general features of hairpin ribozymes are described, e.g., inHampel, et al. (1990) Nucl. Acids Res. 18:299-304; European PatentPublication No. 0 360 257; U.S. Pat. No. 5,254,678. Methods of preparingare well known to those of skill in the art. See, e.g., WO 94/26877;Ojwang, et al. (1993) Proc. Natl. Acad. Sci. USA 90:6340-6344; Yamada,et al. (1994) Human Gene Therapy 1:39-45; Leavitt, et al. (1995) Proc.Natl. Acad. Sci. USA 92:699-703; Leavitt, et al. (1994) Human GeneTherapy 5:1151-120; and Yamada, et al. (1994) Virology 205:121-126.

Polynucleotide modulators of prostate cancer may be introduced into acell containing the target nucleotide sequence by formation of aconjugate with a ligand binding molecule, as described in WO 91/04753.Suitable ligand binding molecules include, but are not limited to, cellsurface receptors, growth factors, other cytokines, or other ligandsthat bind to cell surface receptors. Preferably, conjugation of theligand binding molecule does not substantially interfere with theability of the ligand binding molecule to bind to its correspondingmolecule or receptor, or block entry of the sense or antisenseoligonucleotide or its conjugated version into the cell. Alternatively,a polynucleotide modulator of prostate cancer may be introduced into acell containing the target nucleic acid sequence, e.g., by formation ofan polynucleotide-lipid complex, as described in WO 90/10448. It isunderstood that the use of antisense molecules or knock out and knock inmodels may also be used in screening assays as discussed above, inaddition to methods of treatment.

Thus, in one embodiment, methods of modulating prostate disorders, e.g.,cancer in cells or organisms, are provided. In one embodiment, themethods comprise administering to a patient, e.g., to a cell within thepatient, an anti-prostate cancer antibody that reduces or eliminates thebiological activity of an endogenous prostate cancer protein.Alternatively, the methods comprise administering to a cell or organisma recombinant nucleic acid encoding a prostate cancer protein. This maybe accomplished in many ways. In a preferred embodiment, e.g., when theprostate cancer sequence is down-regulated in prostate cancer, suchstate may be reversed by increasing the amount of prostate cancer geneproduct in the cell. This can be accomplished, e.g., by overexpressingthe endogenous prostate cancer gene or administering a gene encoding theprostate cancer sequence, using known gene-therapy techniques, e.g. In apreferred embodiment, the gene therapy techniques include theincorporation of the exogenous gene using enhanced homologousrecombination (EHR), e.g., as described in PCT/US93/03868, herebyincorporated by reference in its entirety. Alternatively, e.g., when theprostate cancer sequence is up-regulated in prostate cancer, theactivity of the endogenous prostate cancer gene is decreased, e.g., bythe administration of a prostate cancer antisense nucleic acid.

In one embodiment, the prostate cancer proteins of the present inventionmay be used to generate polyclonal and monoclonal antibodies to prostatecancer proteins. Similarly, the prostate cancer proteins can be coupled,using standard technology, to affinity chromatography columns. Thesecolumns may then be used to purify prostate cancer antibodies useful forproduction, diagnostic, or therapeutic purposes. In a preferredembodiment, the antibodies are generated to epitopes unique to aprostate cancer protein; that is, the antibodies show little or nocross-reactivity to other proteins. The prostate cancer antibodies maybe coupled to standard affinity chromatography columns and used topurify prostate cancer proteins. The antibodies may also be used asblocking polypeptides, as outlined above, since they will specificallybind to the prostate cancer protein.

Methods of Identifying Variant Prostate Cancer-Associated Sequences

Without being bound by theory, expression of various prostate cancersequences is correlated with prostate cancer or other prostatedisorders. Accordingly, disorders based on mutant or variant prostatecancer genes may be determined. In one embodiment, the inventionprovides methods for identifying cells containing variant prostatecancer genes, e.g., determining all or part of the sequence of at leastone endogenous prostate cancer genes in a cell. This may be accomplishedusing many sequencing techniques. In a preferred embodiment, theinvention provides methods of identifying the prostate cancer genotypeof an individual, e.g., determining all or part of the sequence of atleast one prostate cancer gene of the individual. This is generally donein at least one tissue of the individual, and may include the evaluationof a number of tissues or different samples of the same tissue. Themethod may include comparing the sequence of the sequenced prostatecancer gene to a known prostate cancer gene, e.g., a wild-type gene.

The sequence of all or part of the prostate cancer gene can then becompared to the sequence of a known prostate cancer gene to determine ifdifferences exist. This can be done using many known homology programs,such as Bestfit, etc. In a preferred embodiment, the presence of adifference in the sequence between the prostate cancer gene of thepatient and the known prostate cancer gene correlates with a diseasestate or a propensity for a disease state, as outlined herein.

In a preferred embodiment, the prostate cancer genes are used as probesto determine the number of copies of the prostate cancer gene in thegenome.

In another preferred embodiment, the prostate cancer genes are used asprobes to determine the chromosomal localization of the prostate cancergenes. Information such as chromosomal localization finds use inproviding a diagnosis or prognosis in particular when chromosomalabnormalities such as translocations, and the like are identified in theprostate cancer gene locus.

Administration of Pharmaceutical and Vaccine Compositions

In one embodiment, a therapeutically effective dose of a prostate cancerprotein or modulator thereof, is administered to a patient. By“therapeutically effective dose” herein is meant a dose that produceseffects for which it is administered. The exact dose will depend on thepurpose of the treatment, and will be ascertainable by one skilled inthe art using known techniques (e.g., Ansel, et al. (1992)Pharmaceutical Dosage Forms and Drug Delivery; Lieberman (1993)Pharmaceutical Dosage Forms (vols. 1-3, Dekker, ISBN 0824770846,082476918X, 0824712692, 0824716981; Lloyd (1999) The Art, Science andTechnology of Pharmaceutical Compounding Amer. Pharma. Assn.; and Pickar(1999) Dosage Calculations Thomson). Adjustments for prostate cancerdegradation, systemic versus localized delivery, and rate of newprotease synthesis, as well as the age, body weight, general health,sex, diet, time of administration, drug interaction, and the severity ofthe condition may be necessary, and will be ascertainable with routineexperimentation by those skilled in the art. U.S. patent applicationSer. No. 09/687,576 further discloses the use of compositions andmethods of diagnosis and treatment in prostate cancer is herebyexpressly incorporated by reference.

A “patient” for the purposes of the present invention includes bothhumans and other animals, particularly mammals. Thus the methods areapplicable to both human therapy and veterinary applications. In thepreferred embodiment the patient is a mammal, preferably a primate, andin the most preferred embodiment the patient is human. The patienttypically will suffer from a prostate proliferative disorder, e.g.,malignant or non-malignant, and may include cancer of other relatedconditions or disorders.

The administration of the prostate cancer proteins and modulatorsthereof of the present invention can be done in a variety of ways asdiscussed above, including, but not limited to, orally, subcutaneously,intravenously, intranasally, transdermally, intraperitoneally,intramuscularly, intrapulmonary, vaginally, rectally, or intraocularly.In some instances, e.g., in the treatment of wounds and inflammation,the prostate cancer proteins and modulators may be directly applied as asolution or spray, or via catheter.

The pharmaceutical compositions of the present invention comprise aprostate cancer protein in a form suitable for administration to apatient. In the preferred embodiment, the pharmaceutical compositionsare in a water soluble form, such as being present as pharmaceuticallyacceptable salts, which is meant to include both acid and base additionsalts. “Pharmaceutically acceptable acid addition salt” refers to thosesalts that retain the biological effectiveness of the free bases andthat are not biologically or otherwise undesirable, formed withinorganic acids such as hydrochloric acid, hydrobromic acid, sulfuricacid, nitric acid, phosphoric acid and the like, and organic acids suchas acetic acid, propionic acid, glycolic acid, pyruvic acid, oxalicacid, maleic acid, malonic acid, succinic acid, fumaric acid, tartaricacid, citric acid, benzoic acid, cinnamic acid, mandelic acid,methanesulfonic acid, ethanesulfonic acid, p-toluenesulfonic acid,salicylic acid, and the like. “Pharmaceutically acceptable base additionsalts” include those derived from inorganic bases such as sodium,potassium, lithium, ammonium, calcium, magnesium, iron, zinc, copper,manganese, aluminum salts, and the like. Particularly preferred are theammonium, potassium, sodium, calcium, and magnesium salts. Salts derivedfrom pharmaceutically acceptable organic non-toxic bases include saltsof primary, secondary, and tertiary amines, substituted amines includingnaturally occurring substituted amines, cyclic amines and basic ionexchange resins, such as isopropylamine, trimethylamine, diethylamine,triethylamine, tripropylamine, and ethanolamine.

The pharmaceutical compositions may also include one or more of thefollowing: carrier proteins such as serum albumin; buffers; fillers suchas microcrystalline cellulose, lactose, corn and other starches; bindingagents; sweeteners and other flavoring agents; coloring agents; andpolyethylene glycol.

The pharmaceutical compositions can be administered in a variety of unitdosage forms depending upon the method of administration. For example,unit dosage forms suitable for oral administration include, but are notlimited to, powder, tablets, pills, capsules and lozenges. It isrecognized that prostate cancer protein modulators (e.g., antibodies,antisense constructs, ribozymes, small organic molecules, etc.) whenadministered orally, should be protected from digestion. This istypically accomplished either by complexing the molecule(s) with acomposition to render it resistant to acidic and enzymatic hydrolysis,or by packaging the molecule(s) in an appropriately resistant carrier,such as a liposome or a protection barrier. Means of protecting agentsfrom digestion are well known in the art.

The compositions for administration will commonly comprise a prostatecancer protein modulator dissolved in a pharmaceutically acceptablecarrier, preferably an aqueous carrier. A variety of aqueous carrierscan be used, e.g., buffered saline and the like. These solutions aretypically sterile and generally free of undesirable matter. Thesecompositions may be sterilized by conventional, well known sterilizationtechniques. The compositions may contain pharmaceutically acceptableauxiliary substances as required to approximate physiological conditionssuch as pH adjusting and buffering agents, toxicity adjusting agents andthe like, e.g., sodium acetate, sodium chloride, potassium chloride,calcium chloride, sodium lactate, and the like. The concentration ofactive agent in these formulations can vary widely, and will be selectedprimarily based on fluid volumes, viscosities, body weight, and the likein accordance with the particular mode of administration selected andthe patient's needs (e.g., (1980) Remington's Pharmaceutical Science(15th ed.); and Hardman, et al. (eds. 2001) Goodman & Gilman: ThePharmacological Basis of Therapeutics McGraw-Hill.

Thus, a typical pharmaceutical composition for intravenousadministration would be about 0.1 to 10 mg per patient per day. Dosagesfrom 0.1 up to about 100 mg per patient per day may be used,particularly when the drug is administered to a secluded site and notinto the blood stream, such as into a body cavity or into a lumen of anorgan. Substantially higher dosages are possible in topicaladministration. Actual methods for preparing parenterally administrablecompositions will be known or apparent to those skilled in the art,e.g., Remington's Pharmaceutical Science and Goodman and Gilman: ThePharmacological Basis of Therapeutics, supra.

The compositions containing modulators of prostate cancer proteins canbe administered for therapeutic or prophylactic treatments. Intherapeutic applications, compositions are administered to a patientsuffering from a disease (e.g., a cancer) in an amount sufficient tocure or at least partially retard or arrest the disease and itscomplications. An amount adequate to accomplish this is defined as a“therapeutically effective dose.” Amounts effective for this use willdepend upon the severity of the disease and the general state of thepatient's health. Single or multiple administrations of the compositionsmay be administered depending on the dosage and frequency as requiredand tolerated by the patient. The composition should provide asufficient quantity of the agents of this invention to effectively treatthe patient. An amount of modulator that is capable of preventing orslowing the development of cancer in a mammal is referred to as a“prophylactically effective dose.” The particular dose required for aprophylactic treatment will depend upon the medical condition andhistory of the mammal, the particular cancer being prevented, as well asother factors such as age, weight, gender, administration route,efficiency, etc. Such prophylactic treatments may be used, e.g., in amammal who has previously had cancer to prevent a recurrence of thecancer, or in a mammal who is suspected of having a significantlikelihood of developing cancer, e.g., based partly on gene expressionprofiles.

It will be appreciated that the present prostate cancerprotein-modulating compounds can be administered alone or in combinationwith additional prostate cancer modulating compounds or with othertherapeutic agent, e.g., other anti-cancer agents or treatments.

In numerous embodiments, one or more nucleic acids, e.g.,polynucleotides comprising nucleic acid sequences set forth in Tables1A-4 such as antisense polynucleotides, silencing RNA, or ribozymes,will be introduced into cells, in vitro or in vivo. The presentinvention provides methods, reagents, vectors, and cells useful forexpression of prostate cancer-associated polypeptides and nucleic acidsusing in vitro (cell-free), ex vivo or in vivo (cell or organism-based)recombinant expression systems.

The particular procedure used to introduce the nucleic acids into a hostcell for expression of a protein or nucleic acid is applicationspecific. Many procedures for introducing foreign nucleotide sequencesinto host cells may be used. These include the use of calcium phosphatetransfection, spheroplasts, electroporation, liposomes, microinjection,plasma vectors, viral vectors, and many other well known methods forintroducing cloned genomic DNA, cDNA, synthetic DNA, or other foreigngenetic material into a host cell (see, e.g., Berger and Kimmel (1987)Guide to Molecular Cloning Techniques from Methods in Enzymology (vol.152) Academic Press; Ausubel, et al., (eds. supplemented through 1999)Current Protocols Lippincott; and Sambrook, et al. (1989) MolecularCloning: A Laboratory Manual (2d ed., Vol. 1-3) CSH Press.

In a preferred embodiment, prostate cancer proteins and modulators areadministered as therapeutic agents, and can be formulated as outlinedabove. Similarly, prostate cancer genes (including both the full-lengthsequence, partial sequences, or regulatory sequences of the prostatecancer coding regions) can be administered in a gene therapyapplication. These prostate cancer genes can include antisenseapplications, either as gene therapy (i.e., for incorporation into thegenome) or as antisense compositions, as will be appreciated by those inthe art.

Prostate cancer polypeptides and polynucleotides can also beadministered as vaccine compositions to stimulate HTL, CTL, and antibodyresponses. Such vaccine compositions can include, e.g., lipidatedpeptides (see, e.g., Vitiello, et al. (1995) J. Clin. Invest.95:341-349), peptide compositions encapsulated inpoly(DL-lactide-co-glycolide) (“PLG”) microspheres (see, e.g., Eldridge,et al. (1991) Molec. Immunol. 28:287-294; Alonso, et al. (1994) Vaccine12:299-306; Jones, et al. (1995) Vaccine 13:675-681), peptidecompositions contained in immune stimulating complexes (ISCOMS) (see,e.g., Takahashi, et al. (1990) Nature 344:873-875; Hu, et al. (1998)Clin Exp Immunol. 113:235-243), multiple antigen peptide systems (MAPs)(see, e.g., Tam (1988) Proc. Natl. Acad. Sci. USA 85:5409-5413; Tam(1996) J. Immunol. Methods 196:17-32), peptides formulated asmultivalent peptides; peptides for use in ballistic delivery systems,typically crystallized peptides, viral delivery vectors (Perkus, et al.,p. 379, in Kaufmann (ed. 1996) Concepts in vaccine development deGruyter; Chakrabarti, et al. (1986) Nature 320:535-537; Hu, et al.(1986) Nature 320:537-540; Kieny, et al. (1986) AIDS Bio/Technology4:790-xxx; Top, et al. (1971) J. Infect. Dis. 124:148-154; Chanda, etal. (1990) Virology 175:535-547), particles of viral or synthetic origin(see, e.g., Kofler, et al. (1996) J. Immunol. Methods 192:25-35;Eldridge, et al. (1993) Sem. Hematol. 30:16-24; Falo, et al. (1995)Nature Med. 7:649-653), adjuvants (Warren, et al. (1986) Annu. Rev.Immunol. 4:369-388; Gupta, et al. (1993) Vaccine 11:293-306), liposomes(Reddy, et al. (1992) J. Immunol. 148:1585-1589; Rock (1996) Immunol.Today 17:131-137), or, naked or particle absorbed cDNA (Ulmer, et al.(1993) Science 259:1745-1749; Robinson, et al. (1993) Vaccine11:957-960; Shiver, et al., p. 423, in Kaufmann (ed. 1996) Concepts inVaccine Development de Gruyter; Cease and Berzofsky (1994) Annu. Rev.Immunol. 12:923-989; and Eldridge, et al. (1993) Sem. Hematol.30:16-24). Toxin-targeted delivery technologies, also known as receptormediated targeting, such as those of Avant Immunotherapeutics, Inc.(Needham, Mass.) may also be used.

Vaccine compositions often include adjuvants. Many adjuvants contain asubstance designed to protect the antigen from rapid catabolism, such asaluminum hydroxide or mineral oil, and a stimulator of immune responses,such as lipid A, Bortadella pertussis or Mycobacterium tuberculosisderived proteins. Certain adjuvants are commercially available as, e.g.,Freund's Incomplete Adjuvant and Complete Adjuvant (Difco Laboratories,Detroit, Mich.); Merck Adjuvant 65 (Merck and Company, Inc., Rahway,N.J.); AS-2 (SmithKline Beecham, Philadelphia, Pa.); aluminum salts suchas aluminum hydroxide gel (alum) or aluminum phosphate; salts ofcalcium, iron or zinc; an insoluble suspension of acylated tyrosine;acylated sugars; cationically or anionically derivatizedpolysaccharides; polyphosphazenes; biodegradable microspheres;monophosphoryl lipid A, and quil A. Cytokines, such as GM-CSF,interleukin-2, -7, -12, and other like growth factors, may also be usedas adjuvants.

Vaccines can be administered as nucleic acid compositions wherein DNA orRNA encoding one or more of the polypeptides, or a fragment thereof, isadministered to a patient. This approach is described, for instance, inWolff, et al. (1990) Science 247:1465-1468 as well as U.S. Pat. Nos.5,580,859; 5,589,466; 5,804,566; 5,739,118; 5,736,524; 5,679,647; WO98/04720; and in more detail below. Examples of DNA-based deliverytechnologies include “naked DNA”, facilitated (bupivicaine, polymers,peptide-mediated) delivery, cationic lipid complexes, andparticle-mediated (“gene gun”) or pressure-mediated delivery (see, e.g.,U.S. Pat. No. 5,922,687).

For therapeutic or prophylactic immunization purposes, the peptides ofthe invention can be expressed by viral or bacterial vectors. Examplesof expression vectors include attenuated viral hosts, such as vacciniaor fowlpox. This approach involves the use of vaccinia virus, e.g., as avector to express nucleotide sequences that encode prostate cancerpolypeptides or polypeptide fragments. Upon introduction into a host,the recombinant vaccinia virus expresses the immunogenic peptide, andthereby elicits an immune response. Vaccinia vectors and methods usefulin immunization protocols are described in, e.g., U.S. Pat. No.4,722,848. Another vector is BCG (Bacille Calmette Guerin). BCG vectorsare described in Stover, et al. (1991) Nature 351:456-460. A widevariety of other vectors useful for therapeutic administration orimmunization, e.g., adeno and adeno-associated virus vectors, retroviralvectors, Salmonella typhi vectors, detoxified anthrax toxin vectors, andthe like, will be apparent to those skilled in the art from thedescription herein (see, e.g., Shata, et al. (2000) Mol. Med. Today6:66-71; Shedlock, et al. (2000) J. Leuk. Biol. 68:793-806; Hipp, et al.(2000) In Vivo 14:571-85).

Methods for the use of genes as DNA vaccines are well known, and includeplacing a prostate cancer gene or portion of a prostate cancer geneunder the control of a regulatable promoter or a tissue-specificpromoter for expression in a prostate cancer patient. The prostatecancer gene used for DNA vaccines can encode full-length prostate cancerproteins, but more preferably encodes portions of the prostate cancerproteins including peptides derived from the prostate cancer protein. Inone embodiment, a patient is immunized with a DNA vaccine comprising aplurality of nucleotide sequences derived from a prostate cancer gene.For example, prostate cancer-associated genes or sequence encodingsubfragments of a prostate cancer protein are introduced into expressionvectors and tested for their immunogenicity in the context of Class IMHC and an ability to generate cytotoxic T cell responses. Thisprocedure may provide for production of cytotoxic T lymphocyte responsesagainst cells which present antigen, including intracellular epitopes.

In a preferred embodiment, the DNA vaccines include a gene encoding anadjuvant molecule with the DNA vaccine. Such adjuvant molecules includecytokines that increase the immunogenic response to the prostate cancerpolypeptide encoded by the DNA vaccine. Additional or alternativeadjuvants are available.

In another preferred embodiment prostate cancer genes find use ingenerating animal models of prostate cancer. When the prostate cancergene identified is repressed or diminished in cancer tissue, genetherapy technology, e.g., wherein antisense RNA directed to the prostatecancer gene will also diminish or repress expression of the gene. Animalmodels of prostate cancer find use in screening for modulators of aprostate cancer-associated sequence or modulators of prostate cancer.Similarly, transgenic animal technology including gene knockouttechnology, e.g., as a result of homologous recombination with anappropriate gene targeting vector, will result in the absence orincreased expression of the prostate cancer protein. When desired,tissue-specific expression or knockout of the prostate cancer proteinmay be necessary.

It is also possible that the prostate cancer protein is overexpressed inprostate cancer. As such, transgenic animals can be generated thatoverexpress the prostate cancer protein. Depending on the desiredexpression level, promoters of various strengths can be employed toexpress the transgene. Also, the number of copies of the integratedtransgene can be determined and compared for a determination of theexpression level of the transgene. Animals generated by such methodsfind use as animal models of prostate cancer and are additionally usefulin screening for modulators to treat prostate cancer.

Kits for Use in Diagnostic and/or Prognostic Applications

For use in diagnostic, research, and therapeutic applications suggestedabove, kits are also provided by the invention. In the diagnostic andresearch applications such kits may include one of the following: assayreagents, buffers, prostate cancer-specific nucleic acids or antibodies,hybridization probes and/or primers, antisense polynucleotides,silencing RNA, ribozymes, dominant negative prostate cancer polypeptidesor polynucleotides, small molecules inhibitors of prostatecancer-associated sequences, etc. A therapeutic product may includesterile saline or another pharmaceutically acceptable emulsion andsuspension base.

In addition, the kits may include instructional materials containinginstructions (i.e., protocols) for the practice of the methods of thisinvention. While the instructional materials typically comprise writtenor printed materials they are not limited to such. A medium capable ofstoring such instructions and communicating them to an end user iscontemplated by this invention. Such media include, but are not limitedto electronic storage media (e.g., magnetic discs, tapes, cartridges,chips), optical media (e.g., CD ROM), and the like. Such media mayinclude addresses to internet sites that provide such instructionalmaterials.

The present invention also provides for kits for screening formodulators of prostate cancer-associated sequences. Such kits can beprepared from readily available materials and reagents. For example,such kits can comprise one or more of the following materials: aprostate cancer-associated polypeptide or polynucleotide, reactiontubes, and instructions for testing prostate cancer-associated activity.Optionally, the kit contains biologically active prostate cancerprotein. A wide variety of kits and components can be prepared accordingto the present invention, depending upon the intended user of the kitand the particular needs of the user. Diagnosis would typically involveevaluation of a plurality of genes or products. The genes will beselected based on correlations with important parameters in diseasewhich may be identified in historical or outcome data.

EXAMPLES Example 1 Gene Chip Analyses of Expression Profiles

Molecular profiles of various normal and cancerous tissues weredetermined and analyzed using gene chips. RNA was isolated and gene chipanalysis was performed as described (Glynne, et al. (2000) Nature403:672-676; Zhao, et al. (2000) Genes Dev. 14:981-993).

Example 2 Identification of Androgen Dependent/Independent Genes

To identify gene expression changes during the transition fromandrogen-dependent to androgen-independent prostate cancer,oligonucleotide microarrays (“K” chips or Affymetrix Eos Hu03) wereinterrogated with cRNAs derived from the human CWR22 prostate cancerxenograft model propagated in nude mice (Pretlow, et al. (1993) J. Natl.Cancer Inst. 85:394-398). The CWR22 xenograft is androgen-dependent whengrown in male Nude mice. Androgen-independent sub-lines can be derivedby first establishing androgen-dependent tumors in male mice. The miceare then castrated to remove the primary source of growth stimulus(androgen), resulting in tumor regression. Within 3-10 months molecularevents prompt the tumors to relapse and start growing asandrogen-independent tumors. See, e.g., Nagabhushan, et al. (1996)Cancer Res. 56:3042-3046; Amler, et al. (2000) Cancer Res. 60:6134-6141;and Bubendorf, et al. (1999) J. Natl. Cancer Inst. 91:1758-1764.

Using the CWR22 xenograft model, tumors were grown subcutaneously inmale nude mice. Tumors were harvested at different times aftercastration. The time points post-castration included (in days): 0, 1, 3,4, 5, 10, 30, 40, 50, 51, 52, 59, 60, 61, 70, 79, 80, 82, 120, and 125.Analyses also included established androgen-independent xenografts.Castration resulted in tumor regression. At day 120 and thereafter, thetumors relapsed and started growing in the absence of androgen.

cRNAs were generated by in vitro transcription assays (IVTs) from thedifferent samples and were hybridized to the oligonucleotide microarrays(Affymetrix Eos Hu03). Hybridization was measured by the averagefluorescence intensity (AI), which is directly proportional to theexpression level of the gene.

Two types of analyses were applied to the results:

Analysis A:

The samples were divided into different time groups which included thefollowing time points post castration (in days): 1-5, 10, 30-40, 50-82,120-125. To identify changes in gene expression, the followingcalculations were made:

1. The median (or mean, in case there were only 2 samples in a group)was calculated for each group.

2. The medians (or means) for each group was compared to one-another.

3. Genes were selected that exhibited a minimum 2 fold difference in themedian (or mean) between any of the groups.

4. The change in gene expression over time was analyzed for eachselected gene to look for specific pattern changes.

Only genes with an interesting expression pattern during theandrogen-ablation time course were selected as potential new therapeutictargets and/or diagnostic markers. Among the 70,000 gene clusterspresent on Hu01 and Hu02, we identified 820 gene clusters with thedesired expression patterns. These expression patterns can be broadlydefined into the following categories:

1. Genes that are expressed early in the time course, then drop off inexpression, and then express again with emergence ofandrogen-independence (hi-lo-hi pattern in Table 1A).

2. Genes that are expressed early in the time course, then drop off inexpression, and do not express again with emergence ofandrogen-independence (hi-lo-lo pattern in Table 1A).

3. Genes that are not expressed early in the time course, but expressonly with emergence of androgen-independence (lo-lo-hi pattern in Table1A).

4. Genes that are not expressed early in the time course, but thenexpress as androgen is withdrawn and continue to express with emergenceof androgen-independence (lo-hi-hi pattern in Table 1A).

5. Genes that are not expressed early in the time course, but thenexpress as androgen is withdrawn and drop off again with emergence ofandrogen-independence (lo-hi-lo pattern in Table 1A).

Group 1 is characterized by cell-cycle regulating genes, such as thoseencoding cyclin B1, p21/WAF1, CDC18-homolog, cyclin A2, cyclin D1, andpossible growth factors such as hAG2 (anterior gradient 2 homolog) amongothers. This indicates that interruption of growth factor and/or cellcycle pathways prevents the emergence of androgen-independent disease,making group 1 genes good targets for treating advanced prostate cancer.

Group 2 represents genes that are androgen-dependent, and do notre-express due to the lack of androgen signal in theandrogen-independent phenotype. This group includes genes encodingproteins such as Fibronectin 1, which has been previously shown to bedown-regulated with androgen-withdrawal (Amler, et al. (2000) CancerRes. 60:6134-6141).

Group 3 represents genes that are up-regulated by signals that inducethe androgen-independent phenotype. This group includes genes encodingstanniocalcin 2, c-fos proto-oncogene product, vascular endothelialgrowth factor, the cell surface protein transmembrane 4 superfamilymember 1 and adrenomedullin among others. Adrenomedullin has recentlybeen shown to act as an autocrine growth factor for theandrogen-independent prostate cancer cell line DU145 (Rocchi, et al.(2001) Cancer Res. 61:1196-1206), indicating that its up-regulation iscritical for supporting an androgen-independent phenotype. Blockingadrenomedullin function, and/or other genes in this group, prevents thegrowth of androgen-independent tumor cells.

Group 4 represents genes that are androgen-repressed and are onlyexpressed in the absence of androgen. This group includes genes encodingthe protein tyrosine phosphatase interacting protein liprin-alpha 2, theCD24 antigen, and the catalytic subunit for phosphatidylinositol4-kinase amongst others. Patients that are treated for advanced prostatecancer by hormone-ablation may have in their bodies cells that havesurvived hormone-ablation and are likely to up-regulate genes thatbelong to Group 4. Therefore, Group 4 gene products are particularlygood therapeutic targets for treating patients undergoinghormone-ablation therapy.

Group 5 represents genes that are involved in regulating signals thatinduce an androgen-independent phenotype. This group includes genesencoding Rab2 (a Ras-like G protein), the Son of Sevenless homolog (aGTP/GDP exchange factor involved in activating Ras-like proteins), andthe p85 regulatory subunit for phosphoinositide-3-kinase (PI3-kinase).The PI3-kinase pathway has been implicated in providing a survivalsignal to the prostate cancer cell line LNCaP (Lin, et al. (1999) CancerRes. 59:2891-2897). This indicates that ras-like signals and signalsdependent on PI3-kinase are involved in inducing theandrogen-independent phenotype. For that reason, Group 5 gene productsare particularly good therapeutic targets for treating patientsundergoing hormone-ablation therapy.

Analysis B:

For the second analysis, the samples were divided into 4 time groupswhich included the following time points post castration (in days):0-1,3-5, 10-82, >120. To identify changes in gene expression, thefollowing analysis was performed:

1. Genes were selected that exhibited a minimum of 100 A1 units at the90^(th) percentile expression level of samples.

2. The group mean expression levels for each gene were calculated. Thegenes were further sub-selected to exhibit a minimum 3 fold differencebetween the group means.

3. An analysis of variance was then performed on selected genes. Fromthe original 59,680 gene clusters present on the Hu03 gene chip, onlyabout 1165 genes with a P value of <0.01 were identified that alsoexhibited the above mentioned parameters.

4. A method was then employed for calculating the positive falsediscovery rate (pFDR), i.e., an estimate of the proportion offalse-positives present in a set of findings (Storey and Tibshirani(2001) Technical Report, Department of Statistics, Stanford University,CA). This technique was developed explicitly for use with microarraydata. The procedure involves randomly assigning the membership status ofeach sample to a group and re-performing the analysis of variance. Ineach simulation, the number of group members (6 for Group 1, 9 for group2, 15 for group 3, and 4 for group 4) remained constant, but thesedesignations were shuffled and assigned to each sample at random. Thepermutation was performed 1000 times, and for each simulation, thenumber of findings at P<0.01 was noted. The number of false positivesunder null conditions, was then divided by the number of actual findings(n=1165 genes) to obtain an estimate of the proportion of false positivefindings. After the application of a correction factor, the finalestimate for the pFDR was about 1%. Thus, one can expect thatapproximately 12 of the 1165 findings are false positives.

5. The approximately 1165 genes were clustered by expression pattern toidentify specific pattern changes. Only genes with an interestingexpression pattern during the androgen-ablation time course wereselected as potential new therapeutic targets and/or diagnostic markers.These expression patterns can be broadly defined into the followingcategories:

1. Genes that are expressed early in the time course of androgenwithdrawal, then drop off in expression, and then express again withemergence of androgen-independence (hi-lo-lo-hi pattern in Table 2A).

2. Genes that are expressed early in the time course, then drop off inexpression immediately after androgen-withdrawal, and do not expressagain with emergence of androgen-independence (hi-lo-lo-lo pattern inTable 2A).

3. Genes that are expressed early in the time course, then drop off inexpression after several days of androgen withdrawal, and do not expressagain with emergence of androgen-independence (hi-hi-lo-lo pattern inTable 2A).

4. Genes that are not expressed early in the time course, but expressonly with emergence of androgen-independence (lo-lo-lo-hi pattern inTable 2A).

5. Genes that are not expressed early in the time course, but thenexpress as androgen is withdrawn and continue to express with emergenceof androgen-independence (lo-lo-hi-hi pattern in Table 2A).

6. Genes that are not expressed early in the time course, but thenexpress as androgen is withdrawn and drop off again with emergence ofandrogen-independence (lo-lo-hi-lo pattern in Table 2A).

Group 1 is characterized by cell-cycle regulating genes and cell growthpromoting genes, such as those encoding cyclin B1 and CDC45 amongothers, growth factors/hormones such as hAG2 (anterior gradient 2homolog), adrenomedullin, and stanniocalcin 2 among others, and growthfactor receptors, such as the bone morphogenic protein receptor type 1B(BMP-R1B) and the endothelial differentiation lysophosphatidic acidG-protein-coupled receptor 7 among others. Adrenomedullin has recentlybeen shown to act as an autocrine growth factor for theandrogen-independent prostate cancer cell line DU145 (Rocchi, et al.(2001) Cancer Res. 61:1196-1206), indicating that its up-regulation iscritical for supporting an androgen-independent phenotype. Thisindicates that interruption of growth factor and/or cell cycle pathwaysprevents the emergence of androgen-independent disease, making group 1genes good targets for treating both localized and advanced prostatecancer and related conditions.

Group 2 represents genes that are androgen-dependent, and do notre-express due to the lack of androgen signal in theandrogen-independent phenotype. This group includes genes encodingproteins such as the endothelial protein C receptor (EPCR) and thepotassium intermediate/small conductance calcium-activated channel(subfamily N, member 2). These genes represent targets for treatingandrogen-dependent prostate cancer and related conditions.

Group 3 also represents genes that are androgen-dependent, and do notre-express due to the lack of androgen signal in theandrogen-independent phenotype. This group includes genes encodingproteins such as Fibronectin 1, which has been previously shown to bedown-regulated with androgen-withdrawal (Amler, et al. (2000) CancerRes. 60:6134-6141), and genes encoding signaling proteins such as RhoGTPase activating protein 1. These genes represent targets for treatingandrogen-dependent prostate cancer and related conditions.

Group 4 represents genes that are up-regulated by signals that induceand maintain the androgen-independent phenotype. This group includesgenes encoding potential growth promoting proteins such aschemokine-like factor (Unigene ID Hs. 15159), colon cancer-associatedprotein Mic1, and the mitogen-activated protein kinase-activated proteinkinase 2. Blocking function of these proteins, and/or other genes inthis group, prevents the growth of androgen-independent tumor cells andrelated conditions.

Group 5 represents genes that are androgen-repressed and are onlyexpressed in the absence of androgen or that are induced by the absenceof androgen. This group includes genes encoding transcriptionalregulators such as the androgen receptor, the DNA activated proteinkinase (catalytic subunit), and nuclear factor related to kappa Bbinding protein (NFRKB), among others. Patients that are treated foradvanced prostate cancer by hormone-ablation may have in their bodiescells that have survived hormone-ablation and are likely to up-regulategenes that belong to Group 5. Therefore, Group 5 gene products areparticularly good therapeutic targets for treating patients undergoinghormone-ablation therapy.

Group 6 represents genes that are involved in regulating signals thatare induced during androgen withdrawal and that induce anandrogen-independent phenotype. This group includes genes encodingsignaling molecules such as phosphoinositide-3-kinase (class 2, alphapolypeptide), signal transducer and activator of transcription 2(STAT2), phospholipase A2 (group IIA) and the protein tyrosinephosphatase interacting protein liprin-alpha 2, cell surface receptorssuch as gamma-aminobutyric acid (GABA) A receptor epsilon subunit,G-protein-coupled receptor 48, and immune function proteins such as themajor histocompatibility complex class II DR alpha. The PI3-kinasepathway has been implicated in providing a survival signal to theprostate cancer cell line LNCaP (Lin, et al. (1999) Cancer Res.59:2891-2897). This indicates that ras-like signals and signalsdependent on PI3-kinase are involved in inducing theandrogen-independent phenotype. For that reason, Group 6 gene productsare particularly good therapeutic targets for treating patientsundergoing hormone-ablation therapy.

TABLE 1A provides Accession numbers for genes, including expressedsequence lags, (incorporated in their entirety here and throughout theapplication where Accession numbers are provided). Genes with aninteresting expression pattern during the androgen-ablation time coursewere selected as potential new therapeutic targets and/or diagnosticmarkers. 820 gene clusters were identified with desired expressionpatterns. These expression patterns can be broadly defined into thefollowing categories:

1. Genes that are expressed early in the time course, then drop off inexpression, and then express again with emergence ofandrogen-independence (hi-lo-hi pattern).

2. Genes that are expressed early in the time course, then drop off inexpression, and do not express again with emergence ofandrogen-independence (hi-lo-lo pattern).

3. Genes that are not expressed early in the time course, but expressonly with emergence of androgen-independence (lo-lo-hi pattern).

4. Genes that are not expressed early in the time course, but thenexpress as androgen is withdrawn and continue to express with emergenceof androgen-independence (lo-hi-hi pattern).

5. Genes that are not expressed early in the time course, but thenexpress as androgen is withdrawn and drop off again with emergence ofandrogen-independence (lo-hi-lo pattern).

Table 1B lists accession numbers for primekeys lacking a unigeneID intable 1A. For each probeset is listed a gene cluster number from whicholigonucleotides were designed. Gene clusters were compiled usingsequences derived from Genbank ESTs and mRNAs. These sequences wereclustered based on sequence similarity using Clustering and AlignmentTools (Double Twist, Oakland Calif.). Genbank accession numbers forsequences comprising each cluster are listed in the “Accession” column.

Table 1C lists genomic positioning for primekeys lacking unigene ID'sand accession numbers in tables 1A. For each predicted exon is listedgenomic sequence source used for prediction. Nucleotide locations ofeach predicted exon are also listed. TABLE 1A Pkey ExAccn UnigeneIDUnigene Title pattern 102772 U83115 Hs.161002 absent in melanoma 1hi-lo-hi 128610 N48373 Hs.10247 activated leucocyte cell adhesion molecuhi-lo-hi 102276 N48373 Hs.10247 activated leucocyte cell adhesion molecuhi-lo-hi 100654 A03758 hi-lo-hi 100655 A03758 hi-lo-hi 135400 X78592Hs.99915 androgen receptor (dihydrotestosterone r hi-lo-hi 331363AW582256 *Hs.91011 anteriror gradient 2 (Xenepus laevis) hom hi-lo-hi115764 AW582256 *Hs.91011 anteriror gradient 2 (Xenepus laevis) homhi-lo-hi 120483 BE251623 Hs.1578 baculoviral IAP repeat-containing 5(sur hi-lo-hi 101505 AA307680 Hs.75692 asparagine synthetase hi-lo-hi127236 AW661857 Hs.98658 budding uninhibited by benzimidazoles 1hi-lo-hi 128472 BE241880 *Hs.10029 cathepsin C hi-lo-hi 102712 U77949Hs.69563 CDC6 (cell division cycle 6, S. cerevisi hi-lo-hi 314943 Y00272Hs.184572 cell division cycle 2, G1 to S and G2 to hi-lo-hi 102123NM_001809 *Hs.1594 centromere protein A (17 kD) hi-lo-hi 326213 CH.17_hsgi|5867224 hi-lo-hi 327110 CH.21_hs gi|6117842 hi-lo-hi 339186CH22_DA59H18.GENSCAN.72-13 hi-lo-hi 337755 CH22_EM:AC000097.GENSCAN.109-2 hi-lo-hi 337674 CH22_EM: AC000097.GENSCAN.67-4hi-lo-hi 337675 CH22_EM: AC000097.GENSCAN.67-6 hi-lo-hi 333516CH22_FGENES.173_1 hi-lo-hi 333517 CH22_FGENES.173_2 hi-lo-hi 333795CH22_FGENES.275_1 hi-lo-hi 333796 CH22_FGENES.275_3 hi-lo-hi 333808CH22_FGENES.279_2 hi-lo-hi 333809 CH22_FGENES.280_2 hi-lo-hi 332792CH22_FGENES.3_2 hi-lo-hi 334101 CH22_FGENES.327_59 hi-lo-hi 334502CH22_FGENES.397_18 hi-lo-hi 334616 CH22_FGENES.411_15 hi-lo-hi 334899CH22_FGENES.452_13 hi-lo-hi 334900 CH22_FGENES.452_14 hi-lo-hi 334902CH22_FGENES.452_16 hi-lo-hi 334905 CH22_FGENES.452_20 hi-lo-hi 334906CH22_FGENES.452_21 hi-lo-hi 334951 CH22_FGENES.465_20 hi-lo-hi 335044CH22_FGENES.480_1 hi-lo-hi 335753 CH22_FGENES.604_2 hi-lo-hi 335755CH22_FGENES.604_4 hi-lo-hi 333135 CH22_FGENES.83_11 hi-lo-hi 333137CH22_FGENES.83_13 hi-lo-hi 333138 CH22_FGENES.83_15 hi-lo-hi 333139CH22_FGENES.83_16 hi-lo-hi 336721 CH22_FGENES.83-17 hi-lo-hi 105012AF098158 Hs.9329 chromosome 20 open reading frame 1 hi-lo-hi 134470X54942 Hs.83758 CDC28 protein kinase 2 hi-lo-hi 134750 L29073 Hs.1139cold shock domain protein A hi-lo-hi 125819 AA044840 *Hs.251871 CTPsynthase hi-lo-hi 102993 BE262998 Hs.85137 cyclin A2 hi-lo-hi 131185BE280074 Hs.23960 cyclin B1 hi-lo-hi 106350 AK001404 *Hs.194698 cyclinB2 hi-lo-hi 103080 AU077231 *Hs.82932 cyclin D1 (PRAD1: peathyroidadenomatos hi-lo-hi 101216 AA284166 Hs.84113 cyclin-dependent kinaseinhibitor 3 (CDK hi-lo-hi 100589 AW247430 Hs.84152cystathionine-beta-synthase hi-lo-hi 130655 AI831962 Hs.17409cysteine-rich protein 1 (intestinal) hi-lo-hi 101473 M22976 Hs.83834cytochrome b-5 hi-lo-hi 101468 BE538296 *Hs.181028 cytochrome c oxidasesubunit Va hi-lo-hi 103546 Z14244 *Hs.75752 cytochrome c oxidase subunitVIIb hi-lo-hi 100829 AA471098 Hs.278544 acetyl-Coenzyme Aacetyltransferase 2 (a hi-lo-hi 102469 AF058293 Hs.180015 D-dopachrometautomerase hi-lo-hi 114292 AI815395 Hs.184641 fatty acid desaturase 2hi-lo-hi 100656 BE250162 *Hs.83765 dihydrofolate reductase hi-lo-hi133799 W24087 Hs.76285 DKFZP5648167 protein hi-lo-hi 129113 BE543205*Hs.288771 DKFZP586A0522 protein hi-lo-hi 332732 AF191019 Hs.8361hypothetical protein, estradiol-induced hi-lo-hi 108846 AL117452*Hs.44155 DKFZP586G1517 protein hi-lo-hi 133903 X63692 *Hs.77462 DNA(cytosine-5-)-methyltransferase 1 hi-lo-hi 320099 AW411307 Hs.114311CDC45 (cell division cycle 45, S. cerevis hi-lo-hi 321960 AA723883Hs.302446 hypothetical protein MGC10334 hi-lo-hi 324988 AK001379*Hs.121028 hypothetical protein FLJ10549 hi-lo-hi 303274 AK001468Hs.62180 anillin (Drosophila Scraps homolog), act hi-lo-hi 301804AK001468 Hs.62180 anillin (Drosophila Scraps homolog), act hi-lo-hi300551 AW408800 Hs.104859 hypothetical protein DKFZp762E1312 hi-lo-hi304541 AA482561 Hs.169476 glyceraldehyde-3-phosphate dehydrogenasehi-lo-hi 304521 AA464716 gb: zx82c11.s1 Soares ovary tumor NbHOT Hhi-lo-hi 129075 BE250162 *Hs.83765 dihydrofolate reductase hi-lo-hi111003 N52980 Hs.83765 dihydrofolate reductase hi-lo-hi 115536 AK001468Hs.62180 anillin (Drosophila Scraps homolog), act hi-lo-hi 108857AK001468 Hs.62180 anillin (Drosophila Scraps homolog). act hi-lo-hi332397 AB027249 Hs.104741 PDZ-binding kinase; T-cell originated prhi-lo-hi 330714 AA263143 Hs.24596 RAD51-interacting protein hi-lo-hi104636 R82252 Hs.106106 Homo sapiens cAMP-dependent protein kinahi-lo-hi 104986 AW088826 Hs.22971 ESTs hi-lo-hi 105076 AI598252 Hs.37810ESTs hi-lo-hi 105312 BE613348 *Hs.23348 S-phase kinase-associatedprotein 2 (p45 hi-lo-hi 105388 AW575008 Hs.11355 thymopoietin hi-lo-hi105953 BE410556 Hs.236556 hypothetical protein STRAIT11499 hi-lo-hi106286 AI765107 *Hs.274422 hypothetical protein FLJ20550 hi-lo-hi 106889U46258 Hs.18349 HSPC145 protein hi-lo-hi 109220 AW958181 Hs.189998 ESTshi-lo-hi 113158 AA328102 Hs.24641 cytoskeleton associated protein 2hi-lo-hi 114542 AW970128 *Hs.293380 ESTs hi-lo-hi 114986 AK000361Hs.133260 hypothetical protein FLJ20354 hi-lo-hi 115291 BE545072*Hs.122579 hypothetical protein FLJ10461 hi-lo-hi 115414 AA662240Hs.283099 AF15q14 protein hi-lo-hi 115471 AK001376 Hs.59346 hypotheticalprotein FLJ10514 hi-lo-hi 115522 BE614387 Hs.47378 ESTs, Moderatelysimilar to T50635 hypot hi-lo-hi 115652 BE093589 Hs.38178 hypotheticalprotein FLJ23468 hi-lo-hi 116121 AK001330 Hs.48855 hypothetical proteinFLJ10468 hi-lo-hi 116130 AW183533 Hs.38178 hypothetical protein FLJ23468hi-lo-hi 116448 BE268321 Hs.208912 hypothetical protein MGC861 hi-lo-hi116787 AW362955 Hs.15641 ESTs hi-lo-hi 118336 BE327311 Hs.47166 HT021hi-lo-hi 120649 AA687322 Hs.192843 leucine zipper protein FKSG14hi-lo-hi 121503 AA412049 Hs.290347 ESTs hi-lo-hi 121748 BE536911Hs.234545 Homo sapiens NUF2R mRNA, complete cds hi-lo-hi 122860 AA464414gb: zx78g01.s1 Soares ovary tumor NbHOT H hi-lo-hi 123477 AF217515Hs.283532 uncharacterized bone marrow protein BM03 hi-lo-hi 130338AI375726 *Hs.279918 hypothetical protein hi-lo-hi 130680 BE567313Hs.183109 monoamine oxidase A hi-lo-hi 131148 AW953575 *Hs.303125p53-induced protein PIGPC1 hi-lo-hi 131626 BE514805 *Hs.289092 Homosapiens cDNA: FLJ22380 fis, clone H hi-lo-hi 131937 AI907735 Hs.21446Homo sapiens mRNA for KIAA1716 protein, hi-lo-hi 131965 W79283 Hs.35962ESTs hi-lo-hi 132371 AA235448 Hs.46677 PRO2000 protein hi-lo-hi 133626AW836130 Hs.75277 hypothetical protein FLJ13910 hi-lo-hi 300942 AW301344Hs.122908 Homo sapiens, clone IMAGE: 3048353, mRNA, hi-lo-hi 300953AA542845 Hs.294088 ESTs hi-lo-hi 302656 BE090580 Hs.70704 Homo sapiens,clone IMAGE: 2823731, mRNA, hi-lo-hi 311928 T62216 Hs.270840 ESTshi-lo-hi 313637 AK000742 Hs.126774 L2DTL protein hi-lo-hi 313832AW271106 Hs.133294 ESTs hi-lo-hi 316465 AW574774 Hs.121692 ESTs hi-lo-hi317202 AA894880 Hs.181181 ESTs hi-lo-hi 320771 R74441 Hs.117176poly(A)-binding protein, nuclear 1 hi-lo-hi 321636 AI820961 Hs.193465ESTs hi-lo-hi 330867 AW978991 Hs.221197 ESTs hi-lo-hi 331442 H77381Hs.159420 ESTs hi-lo-hi 106654 AW075485 Hs.286049 phosphoserineaminotransferase hi-lo-hi 106590 AI350260 Hs.301539 hypothetical proteinMGC2633 hi-lo-hi 128460 T16206 Hs.237164 ESTs, highly similar toLDHH_HUMAN L-LA hi-lo-hi 114394 T34462 Hs.103291 neuritin hi-lo-hi315936 AW069807 Hs.271252 ESTs hi-lo-hi 108886 AW248434 Hs.91521hypothetical protein hi-lo-hi 129241 AI878857 Hs.109706 hematologicaland neurological expressed hi-lo-hi 104978 AI199268 Hs.19322 ESTs,Weakly similar to CGHU7L collagen hi-lo-hi 129626 F13272 Hs.111334ferritin, light polypeptide hi-lo-hi 118895 BE304917 Hs.31097hypothetical protein FLJ21478 hi-lo-hi 332577 AI826268 Hs.27769 ESTs,Weakly similar to MCAT_HUMAN MITOC hi-lo-hi 116732 AW152225 Hs.165909ESTs hi-lo-hi 106774 AI216748 Hs.14587 ESTs, Weakly similar AF151859 1CGI-1 hi-lo-hi 108818 BE612676 Hs.303116 stromal cell-derived factor2-like 1 hi-lo-hi 315618 AI287341 *Hs.154029 bHLH factor Hes4 hi-lo-hi110561 AA379597 Hs.5199 HSPC150 protein similar to ubiquitin-conhi-lo-hi 132959 AW014195 Hs.61472 ESTs, Weakly similar to unknown [S.cerev hi-lo-hi 103195 AA351647 Hs.2642 eukaryotic translation elongationfactor hi-lo-hi 100368 D79987 Hs.153479 extra spindle poles, S.cerevisiae, homo hi-lo-hi 103177 BE244377 *Hs.48876 farnesyl-diphosphatefarnesyltransferase hi-lo-hi 109141 AF174600 Hs.193380 F-box proteinFbx20 hi-lo-hi 100676 X02761 *Hs.287820 fibronectin 1 hi-lo-hi 100254AA452181 Hs.77643 FK506-binding protein 1B (12.6 kD) hi-lo-hi 133688U71321 Hs.7557 FK506-binding protein 5 hi-lo-hi 107129 AC004770 *Hs.4756flap structure-specific endonuclease 1 hi-lo-hi 102696 BE540274 Hs.239forkhead box M1 hi-lo-hi 101753 L11144 Hs.1907 galanin hi-lo-hi 101597AA317089 *Hs.597 glutamic-oxaloacetic transaminase 1, sol hi-lo-hi133512 L18861 gb: Human Golli-mbp gene, exon 1 hi-lo-hi 130080 X14850Hs.147097 H2A histone family, member X hi-lo-hi 101600 BE561617*Hs.119192 H2A histone family, member Z hi-lo-hi 101332 J04088*Hs.156346 topoisomerase (DNA) II alpha (170 kD) hi-lo-hi 132967AA316181 Hs.61635 six transmembrane epithelial antigen of hi-lo-hi129726 H15474 Hs.132898 fatty acid desaturase 1 hi-lo-hi 106925 AK002011Hs.37558 hypothetical protein FLJ11149 hi-lo-hi 105643 BE621719Hs.173802 KIAA0603 gene product hi-lo-hi 116028 H59799 Hs.42644thioredoxin-like hi-lo-hi 105437 AF151076 Hs.25199 hypothetical proteinhi-lo-hi 122512 AF053305 Hs.98658 budding uninhibited by benzimidazoles1 hi-lo-hi 131991 AF053306 Hs.36708 budding uninhibited bybeuzimidazoles 1 hi-lo-hi 135015 AW361638 Hs.278338 LGN protein hi-lo-hi102208 U22961 gb: Human mRNA clone with similarity to L hi-lo-hi 100144AL119964 Hs.75616 seladin-1 hi-lo-hi 100447 NM_014767 Hs.74583 KIAA0275gene product hi-lo-hi 116578 D21262 Hs.75337 nucleolar phosphoproteinp130 hi-lo-hi 130350 AA369601 Hs.239138 pre-B-cell colony-enhancingfactor hi-lo-hi 101045 J05614 gb: Human proliferating cell nuclear antihi-lo-hi 101544 M31169 gb: Human propionyl-CoA carboxylase beta-hi-lo-hi 113674 NM_014214 Hs.5753 inositol(myo)-1(or 4)-monophosphatase2 hi-lo-hi 102260 AL039104 Hs.159557 karyopherin alpha 2 (RAG cohort 1,impor hi-lo-hi 100154 H60720 Hs.81892 KIAA0101 gene product hi-lo-hi100199 BE562298 Hs.71827 KIAA0112 protein; homolog of yeast riboshi-lo-hi 100372 NM_014791 Hs.184339 KIAA0175 gene product hi-lo-hi100387 D83777 *Hs.75137 K1AA0193 gene product hi-lo-hi 131514 BE270734*Hs.2795 lactate dehydrogenase A hi-lo-hi 102938 W27518 Hs.234489lactate dehydrogenase B hi-lo-hi 105811 BE617695 Hs.286192 proteinphosphatase 1, regulatory (inhib hi-lo-hi 101013 BE300094 *Hs.227751lectin, galactoside-binding, soluble, 1 hi-lo-hi 124148 BE300094*Hs.227751 lectin, galactoside-binding, soluble, 1 hi-lo-hi 102968AU076611 Hs.154672 methylene tetrahydrofolate dehydrogenase hi-lo-hi130149 AW067805 Hs.172665 methylenetetrahydrofolate dehydrogenasehi-lo-hi 114767 AI859865 Hs.154443 minichromosome maintenance deficient(S. hi-lo-hi 129168 AI132988 Hs.109052 chromosome 14 open reading frame2 hi-lo-hi 105011 BE091926 Hs.16244 mitotic spindle coiled-coil relatedprot hi-lo-hi 103023 AW500470 Hs.117950 multifunctional polypeptidesimilar to S hi-lo-hi 102808 BE242818 *Hs.179606 nuclear RNA helicase,DECD variant of DE hi-lo-hi 318617 AW247252 Hs.75514 nucleosidephosphorylase hi-lo-hi 101568 M81740 Hs.75212 ornithine decarboxylase 1hi-lo-hi 102076 BE299197 Hs.179665 cyclin-dependent kinase inhibitor 1A(p2 hi-lo-hi 100202 BE294407 *Hs.99910 phosphofructokinase, platelethi-lo-hi 101032 BE206854 Hs.46039 phosphoglycerate mutase 2 (muscle)hi-lo-hi 130553 AF062649 *Hs.252587 pituitary tumor-transforming 1hi-lo-hi 101626 M57399 Hs.44 pleiotrophin (heparin binding growth fachi-lo-hi 101992 X90725 Hs.77597 polo (Drosophia)-like kinase hi-lo-hi132164 AI752235 Hs.41270 procollagen-lysine, 2-oxoglutarate 5-diohi-lo-hi 101396 BE267931 *Hs.78996 proliferating cell nuclear antigenhi-lo-hi 119018 AA631143 Hs.179809 ESTs hi-lo-hi 101840 AA236291Hs.183583 sense (or cysteine) proteinase inhibito hi-lo-hi 332640BE568452 Hs.5101 protein regulator of cytokinesis 1 hi-lo-hi 132543BE568452 Hs.5101 protein regulator of cytokinesis 1 hi-lo-hi 101118AA371931 *Hs.77422 proteolipid protein 2 (colonic epitheliu hi-lo-hi109166 AA219691 Hs.73625 RAB6 interacting, kinesis-like (rabkineshi-lo-hi 100830 AC004770 *Hs.4756 flap structure-specific endonuclease 1hi-lo-hi 107059 BE614410 Hs.23044 RAD51 (S. cerevisiae) homolog (E coliRe hi-lo-hi 321693 AA227069 Hs.173737 ras-related C3 botulinum toxinsubstrate hi-lo-hi 101148 NM_002923 Hs.78944 regulator of G-proteinsignaling 2, 24 k hi-lo-hi 130567 AA383092 Hs.1608 replication proteinA3 (14 kD) hi-lo-hi 103076 NM_001034 Hs.75319 ribonucleotide reductaseM2 polypeptide hi-lo-hi 103131 BE536069 Hs.2962 S100 calcium-bindingprotein P hi-lo-hi 102212 AW411491 Hs.75069 serinehydroxymethyltransferase 2 (mitoc hi-lo-hi 104254 AW411425 Hs.180655serine/threonine kinase 12 hi-lo-hi 102748 BE018138 Hs.24447 sigmareceptor (SR31747 binding protein hi-lo-hi 102012 BE259035 Hs.118400singed (Drosophila)-like (sea urchin fas hi-lo-hi 102522 BE250944Hs.183556 solute carrier family 1 (neutral amino a hi-lo-hi 132994AA112748 Hs.279905 clone HQ0310 PRO0310p1 hi-lo-hi 101971 Z49105*Hs.289105 synovial sarcoma, X breakpoint 2 hi-lo-hi 126645 AA316181Hs.61635 six transmembrane epithelial antigen of hi-lo-hi 103058 X57348Hs.184510 stratifin hi-lo-hi 102632 U66618 Hs.250581 SWI/SNF related,matrix associated, acti hi-lo-hi 103269 AF230662 *Hs.289105 synovialsarcoma, X breakpoint 2 hi-lo-hi 128920 AA622037 Hs.166468 programmedcell death 5 hi-lo-hi 100114 X02308 Hs.82962 thymidylate synthetasehi-lo-hi 102846 BE264974 Hs.6566 thyroid hormone receptor interector 13hi-lo-hi 131877 J04088 *Hs.156346 topoisomerase (DNA) II alpha (170 kD)hi-lo-hi 100866 U14134 Hs.75113 general transcription factor IIIAhi-lo-hi 133893 AI434699 Hs.77356 transferrin receptor (p90, CD71)hi-lo-hi 130135 AA311426 *Hs.21635 tubulin, gamma 1 hi-lo-hi 130287AA479005 Hs.154036 tumor suppressing subtransferable candid hi-lo-hi126180 L32977 Hs.3712 ubiquinol-cytochrome c reductase, Rieske hi-lo-hi101536 NM_006002 Hs.77917 ubiquitin carboxyl-terminal esterase L3hi-lo-hi 102687 NM_007019 *Hs.93002 ubiquitin carrier protein E2-Chi-lo-hi 103556 Z19002 Hs.37096 zinc finger protein 145 (Kruppel-liKe, ehi-lo-hi 300022 hi-lo-hi-lo 133015 AJ002744 Hs.246315UDP-N-acetyl-alpha-D-galactosamine:polyp hi-lo-hi-lo 129642 NM_001360Hs.11806 7-dehydrocholesterol reductase hi-lo-hi-lo 134369 AF207664Hs.8230 a disintegrin-like and metatlloprotease ( hi-lo-lo 300023hi-lo-lo 125183 AV660804 Hs.301417 AHNAK nucleoprotein (desmoyokin)hi-lo-lo 101766 M80899 *Hs.301417 AHNAK nucleoprotein (desmoyokin)hi-lo-lo 133516 BE265133 *Hs.217493 annexin A2 hi-lo-lo 102146 AW162057Hs.78629 ATPase, Na+/K+ transporting, beta 1 poly hi-lo-lo 318538AI750979 Hs.74034 Homo sapiens clone 24651 mRNA sequence hi-lo-lo 103554AI878826 Hs.323469 caveolin 1, caveolae protein, 22 KD hi-lo-lo 329365CH.X_hs gi|5868838 hi-lo-lo 334282 CH22_FGENES.369_12 hi-lo-lo 334891CH22_FGENES.452_5 hi-lo-lo 335149 CH22_FGENES.499_5 hi-lo-lo 335682CH22_FGENES.595_2 hi-lo-lo 335756 CH22_FGENES.604_5 hi-lo-lo 303951AW475081 Hs.172928 collagen, type I, alpha 1 hi-lo-lo 134421 AU077196Hs.82985 collagen, type V, alpha 2 hi-lo-lo 131101 BE387561 Hs.22981DKFZP586M1523 protein hi-lo-lo 124153 AU077333 *Hs.160483 erythrocytemembrane protein band 7.2 (s hi-lo-lo 103328 AU077333 *Hs.160483erythrocyte membrane protein band 7.2 (s hi-lo-lo 322035 AL137517*Hs.306201 hypothetical protein DKFZp564O1278 hi-lo-lo 301872 H84730Hs.326391 ESTs, Highly similar to KIAA1437 protein hi-lo-lo 303820AB037858 Hs.173484 hypothetical protein FLJ10337 hi-lo-lo 304049 T58155gb: yb98h03.s1 Stratagene lung (937210) H hi-lo-lo 304735 AA576453 gb:nm75h11.s1 NCl_CGAP_Co9 Homo sapiens hi-lo-lo 306999 AI138628 Hs.308058EST, Weakly similar to zinc finger prot hi-lo-lo 128789 AW368576Hs.139851 caveolin 2 hi-lo-lo 132057 AB037858 Hs.173484 hypotheticalprotein FLJ10337 hi-lo-lo 114795 AB037858 Hs.173484 hypothetical proteinFLJ10337 hi-lo-lo 104204 AK001691 Hs.57655 hypothetical protein FLJ10829hi-lo-lo 105200 AA328102 Hs.24641 cytoskeleton associated protein 2hi-lo-lo 105493 AL047586 Hs.10283 RNA binding motif protein 8B hi-lo-lo107977 AI188161 Hs.144627 ESTs hi-lo-hi 108880 AA766606 *Hs.47099hypothetical protein FLJ21212 hi-lo-lo 111157 AL109729 Hs.18948 ESTs,Highly similar to A31026 probable hi-lo-lo 116202 BE159395 Hs.87089 ESTshi-lo-lo 120689 AW134519 Hs.96125 ESTs hi-lo-lo 121847 AA446628 Hs.2799cartilage linking protein 1 hi-lo-lo 124182 AI637471 Hs.107801 ESTshi-lo-lo 128515 BE395085 Hs.10086 type I transmembrane protein Fn14hi-lo-lo 130466 W19744 Hs.180059 Homo sapiens cDNA FLJ20653 fis, cloneKA hi-lo-lo 131076 AA749230 Hs.22666 ESTs hi-lo-lo 131084 NM_017413Hs.303084 apelin; peptide ligand for APJ receptor hi-lo-lo 134109AA348031 Hs.7913 ESTs hi-lo-lo 300258 AI478933 Hs.188260 ESTs hi-lo-lo302767 H94900 Hs.17882 ESTs hi-lo-lo 312391 R43707 Hs.133159 ESTs,Weakly similar to PIHUSD salivary hi-lo-lo 312689 AW450461 Hs.203965ESTs hi-lo-lo 315715 AI284219 Hs.130749 ESTs hi-lo-lo 315843 AA679430Hs.191897 ESTs hi-lo-lo 322447 AI735759 Hs.52620 integrin, beta 8hi-lo-lo 322826 AI807883 Hs.201771 ESTs hi-lo-lo 324867 AI624707*Hs.5921 Homo sapiens cDNA: FLJ21592 fis, clone C hi-lo-lo 331336AA287450 Hs.93842 Homo sapiens cDNA: FLJ22554 fis, clone hi-lo-lo 331353AA953006 Hs.88143 ESTs hi-lo-lo 133063 AI654133 Hs.30212 thyroidreceptor interacting protein 15 hi-lo-lo 311034 BE567130 Hs.311389 ESTs,Moderately similar to PT0375 natur hi-lo-lo 108647 BE546947 Hs.44276hameo box C10 hi-lo-lo 124955 AA376768 *Hs.324841 hypothetical proteinFLJ22622 hi-lo-lo 113923 AW953484 Hs.3849 hypothetical protein FLJ22041similar to hi-lo-lo 310557 AI431798 Hs.164192 ESTs, Weakly similar toY161_HUMAN HYPOT hi-lo-lo 302943 AI581344 Hs.127812 ESTs, Weakly similarto T17330 hypotheti hi-lo-lo 128453 X02761 *Hs.287820 fibronectin 1hi-lo-lo 305232 AA670052 Hs.169476 glyceraldehyde-3-phosphatedehydrogenase hi-lo-lo 117642 U55184 *Hs.154145 hypothetical proteinFLJ11585 hi-lo-lo 115881 NM_005756 Hs.184942 G protein-coupled receptor64 hi-lo-lo 133666 U56725 Hs.75452 heat shock 70 kD protein 2 hi-lo-lo103262 X78565 Hs.289114 hexabrachion (tenascin C, cytotactin) hi-lo-lo100793 S69027 gb: HOX C6 = class I homeodomain (fragment hi-lo-lo 102289U32114 hi-lo-lo 319109 Z45662 Hs.90797 Homo sapiens clone 23620 mRNAsequence hi-lo-lo 116357 AF052107 Hs.90797 Homo sapiens clone 23620 mRNAsequence hi-lo-lo 101497 W05150 *Hs.37034 homeo box A5 hi-lo-lo 105508AA173942 Hs.326416 Homo sapiens mRNA; cDNA DKFZp564H1916 (f hi-lo-lo302290 AA179949 Hs.175563 Homo sapiens mRNA: cDNA DKFZp564N0763 (fhi-lo-lo 102838 R34657 Hs.80658 uncoupling protein 2 (mitochondrial, prohi-lo-lo 100235 D29954 Hs.13421 KIAA0056 protein hi-lo-lo 133507NM_002206 Hs.74369 integrin, alpha 7 hi-lo-lo 125573 AI351642 Hs.182241interferon induced transmembrane protein hi-lo-lo 103059 X57351Hs.174195 interferon induced transmembrane protein hi-lo-lo 330415D83777 *Hs.75137 KIAA0193 gene product hi-lo-lo 303054 BE265848Hs.289080 colon cancer-associated protein Mic1 hi-lo-lo 133579 X75346Hs.75074 mitogen-activated protein kinase-activat hi-lo-lo 100528BE386801 Hs.21858 trinucleotide repeat containing 3 hi-lo-lo 107480AF001691 Hs.74304 periplakin hi-lo-lo 133050 X73424 Hs.63788 propionylCoenzyme A carboxylase, beta p hi-lo-lo 133061 AI186431 Hs.296638prostate differentiation factor hi-lo-lo 106390 AJ297436 Hs.20166prostate stem cell antigen hi-lo-lo 302124 AA676403 Hs.145078 regulatorof differentiation (in S. pomb hi-lo-lo 129823 X00949 *Hs.105314 relaxin1 (H1) hi-lo-lo 134444 BE184455 *Hs.251754 secretory leukocyte proteaseinhibitor ( hi-lo-lo 103240 U81961 Hs.2794 sodium channel,nonvoltage-gated 1 alpha hi-lo-lo 115761 AA366037 Hs.90911 solutecarrier family 16 (monocarboxylic hi-lo-lo 321412 AI674383 Hs.22891solute carrier family 7 (cationic amino hi-lo-lo 126487 AA283809Hs.184601 solute carrier family 7 (cationic amino hi-lo-lo 101759 M80244Hs.184601 solute carrier family 7 (cationic amino hi-lo-lo 112941AW163034 Hs.6467 synaptogyrin 3 hi-lo-lo 134351 BE272506 *Hs.82109syndecan 1 hi-lo-lo 125924 BE272506 *Hs.82109 syndecan 1 hi-lo-lo 130982AA033627 Hs.21858 trinucleotide repeat containing 3 hi-lo-lo 133473AW301993 Hs.73980 troponin T1, skeletal, slow hi-lo-lo 101042 T46839*Hs.10319 UDP glycosyltransferase 2 family, polype hi-lo-lo 129565X77777 Hs.198726 vasoactive intestinal peptide receptor 1 hi-lo-lo102992 M85430 *Hs.155191 villin 2 (ezrin) hi-lo-lo 106868 BE185536Hs.300816 Homo sapiens mRNA; cDNA DKFZp564I172 (fr lo-hi-lo 132618AL050025 *Hs.279916 hypothetical protein FLJ20151 lo-hi-hi 100187 D17793*Hs.78183 aldo-keto reductase family 1, member C3 lo-hi-hi 116334AL038450 Hs.48948 ATP2C1 calcium transport ATPase, same as lo-hi-hi134454 NM_013230 Hs.286124 CD24 antigen (small cell lung carcinomalo-hi-hi 302067 BE542706 Hs.222399 CEGP1 protein lo-hi-hi 105500AW602166 Hs.222399 CEGP1 protein lo-hi-hi 100732 AA557660 *Hs.76152decorin lo-hi-hi 129265 AA530892 Hs.171695 dual specificity phosphatase1 lo-hi-hi 117789 N48294 Hs.46850 EST lo-hi-hi 330786 BE379594 *Hs.49136ESTs, Moderately similar to ALU7_HUMAN A lo-hi-hi 319808 T58960 Hs.17283hypothetical protein FLJ10890 lo-hi-hi 303502 BE174240 gb:QV1-HT0573-290200-092-106 HT0573 Homo lo-hi-hi 116780 H22566 *Hs.30098ESTs lo-hi-hi 104189 AB040927 Hs.301804 KIAA1494 protein lo-hi-hi 105588L43821 Hs.80261 enhancer of filamentation 1, (cas-like do lo-hi-hi105731 AA834664 Hs.29131 nuclear receptor coactivator 2 lo-hi-hi 105772H57111 Hs.221132 ESTs lo-hi-hi 105794 H24530 Hs.273294 hypotheticalprotein FLJ20069 lo-hi-hi 113098 N77737 Hs.8349 Apobec-1 complementationfactor; APOBEC- lo-hi-hi 113803 AW880709 *Hs.283683 chromosome 8 openreading frame 4 lo-hi-hi 114530 AA601038 Hs.191797 ESTs lo-hi-hi 116188AA468183 Hs.184598 Homo sapiens cDNA; FLJ23241 fis, clone C lo-hi-hi117330 AI904095 Hs.43423 ESTs lo-hi-hi 117701 BE063921 Hs.295971 ESTslo-hi-hi 120911 AI189754 Hs.144330 ESTs lo-hi-hi 124083 AW195237 Hs.7734hypothetical protein FLJ22174 lo-hi-hi 124690 AW883529 Hs.173830 ESTslo-hi-hi 130796 AA088809 Hs.19525 hypothetical protein FLJ22794 lo-hi-hi131524 AB040927 Hs.301804 KIAA1494 protein lo-hi-hi 132116 AW960474Hs.40289 ESTs lo-hi-hi 132442 AW970859 Hs.313503 ESTs lo-hi-hi 310219AI221087 Hs.147761 ESTs lo-hi-hi 310598 AI439136 Hs.140546 ESTs lo-hi-hi310884 AW014684 Hs.232189 ESTs lo-hi-hi 311587 AI828254 Hs.271019 ESTs,Weakly similar to SMN1_HUMAN SURVI lo-hi-hi 312240 R36475 Hs.24321 Homosapiens cDNA FLJ12028 fis, clone HE lo-hi-hi 312803 AA677934 Hs.117864ESTs lo-hi-hi 314219 AA262331 Hs.48376 Homo sapiens clone HB-2 mRNAsequence lo-hi-hi 315052 AA876910 Hs.134427 ESTs lo-hi-hi 331919AA446869 Hs.119316 ESTs lo-hi-hi 133240 AK001489 Hs.242894ADP-ribosylation factor-like 1 lo-hi-hi 134006 Z45957 Hs.7837G-protein-coupled receptor induced prote lo-hi-hi 124847 W07701*Hs.304177 Homo sapiens clone FLB8503 PRO2286 mRNA, lo-hi-hi 129087AI348027 Hs.108557 Homo sapiens clone PP1057 unknown mRNA lo-hi-hi131762 AA744902 *Hs.107767 hypothetical protein PRO1489 lo-hi-hi 129000AA744902 *Hs.107767 hypothetical protein PRO1489 lo-hi-hi 105713AI122843 *Hs.184319 ESTs, Weakly similar to KIAA1006 protein lo-hi-hi118475 N66845 gb: za46c11.s1 Soares fetal liver spleen lo-hi-hi 118381N64513 Hs.48994 ESTs, Weakly similar to AF151800 1 CGI-4 lo-hi-hi 105057AA134233 gb: zo20f10.s1 Stratagene colon (937204) lo-hi-hi 131507AI826268 Hs.27769 ESTs, Weakly similar to MCAT_HUMAN MITOC lo-hi-hi124970 BE272862 Hs.106534 hypothetical protein FLJ22625 lo-hi-hi 130094NM_001471 *Hs.167017 gamma-aminobutyric acid (GABA) B recepto lo-hi-hi302357 X03178 Hs.198246 group-specific component (vitamin D bindlo-hi-hi 113231 AA278583 Hs.180737 Homo sapiens clone 23664 and 23905mRNA lo-hi-hi 111923 BE383234 Hs.25925 Homo sapiens clone 23860 mRNAsequence lo-hi-hi 128530 AI932995 Hs.183475 Homo sapiens clone 25061mRNA sequence lo-hi-hi 128987 AI339046 Hs.107637 hypothetical proteinFLJ12806 lo-hi-hi 315368 AB037745 Hs.104696 KIAA1324 protein lo-hi-hi133944 AW068579 Hs.7780 Homo sapiens mRNA; cDNA DKFZp564A072 (frlo-hi-hi 115084 BE383668 *Hs.42484 hypothetical protein FLJ10618lo-hi-hi 132883 AA373314 Hs.5897 Homo sapiens mRNA; cDNA DKFZp586P1622(f lo-hi-hi 109623 AW207385 Hs.295901 KIAA0493 protein lo-hi-hi 130577M69241 *Hs.162 insulin-like growth factor binding prote lo-hi-hi 101889AF188747 *Hs.181350 kallikrein 2, prostatic lo-hi-hi 130336 AA535210*Hs.171995 kallikrein 3, (prostate specific antigen lo-hi-hi 128180AW949068 Hs.171995 kallikrein 3, (prostate specific antigen lo-hi-hi134921 AL137491 Hs.125511 Homo sapiens mRNA; cDNA DKFZp434P1530 (flo-hi-hi 302385 AJ224172 Hs.204096 lipophilin B (uteroglobin familymember) lo-hi-hi 117921 AA021459 Hs.306480 Homo sapiens mRNA; cDNADKFZp761E2112 (f lo-hi-hi 101701 NM_002436 Hs.1861 membrane protein,palmitoylated 1 (55 kD) lo-hi-hi 130356 AF127577 Hs.155017 nuclearreceptor interacting protein 1 lo-hi-hi 101763 AB001914 Hs.170414 pairedbasic amino acid cleaving system lo-hi-hi 130342 U81802 Hs.154846phosphatidylinositol 4-kinase, catalytic lo-hi-hi 130760 AW379130Hs.18953 phosphodiesterase 9A lo-hi-hi 101461 N98569 Hs.76422phospholipase A2, group IIA (platelets, lo-hi-hi 134032 NM_005025Hs.78589 serine (or cysteine) proteinase inhibito lo-hi-hi 303762AF034799 Hs.30881 protein tyrosine phosphatase, receptor t lo-hi-hi110932 AA021459 Hs.306480 Homo sapiens mRNA; cDNA DKFZp761E2112 (flo-hi-hi 135192 U83993 Hs.321709 purinergic receptor P2X, ligand-gatedio lo-hi-hi 133886 U97276 Hs.77266 quiescin Q6 lo-hi-hi 134142 BE244053Hs.79362 retinoblastoma-like 2 (p130) lo-hi-hi 100877 X80821 Hs.302177H. sapiens mRNA for ribosomal protein L18 lo-hi-hi 133534 AU077115Hs.201675 RNA binding motif protein 5 lo-hi-hi 133011 NM_006379Hs.171921 sema domain, immunoglobulin domain (Ig), lo-hi-hi 132160W26406 Hs.295923 seven in absentia (Drosophila) homolog 1 lo-hi-hi103110 X62822 Hs.2554 sialyltransferase 1 (beta-galactoside al lo-hi-hi130173 U38847 Hs.151518 TAR (HIV) RNA-binding protein 1 lo-hi-hi 127435X69086 *Hs.286161 Homo sapiens cDNA FLJ3613 fis, clone PL lo-hi-hi110520 N54069 Hs.4082 lectin, galactoside-binding, soluble, 8 lo-hi-hi114660 AA071383 gb: zm61d05.r1 Stratagene fibroblast (937 lo-hi-hi330541 NM_002038 Hs.265827 interferon, alpha-inducible protein (clolo-hi-lo 101486 AA506324 Hs.1852 acid phosphatase, prostate lo-hi-lo332386 NM_000481 Hs.102 aminomethyltransferase (glycine cleavagelo-hi-lo 100569 AA535210 *Hs.171995 kallikrein 3, (prostate specificantigen lo-hi-lo 134738 AU076801 Hs.89436 cadherin 17, LI cadherin(liver-intestin lo-hi-lo 103119 X63629 Hs.2877 cadherin 3, type 1,P-cadherin (placenta lo-hi-lo 302892 AW176909 Hs.42346calcineurin-binding protein calsarcin-1 lo-hi-lo 105402 AB014680 Hs.8786carbohydrate (chondroitin 6/keratan) su$$ lo-hi-lo 102976 AU077174*Hs.288181 cathepsin H lo-hi-lo 101793 W01076 *Hs.119663 CD59 antigenp18-20 (antigen identified lo-hi-lo 129890 AI868872 *Hs.282804 Homosapiens cDNA; FLJ22704 fis, clone H lo-hi-lo 328164 CH.06_hs gi|5868068lo-hi-lo 328648 CH.07_hs gi|6004473 lo-hi-lo 330032 CH.16_p2 gi|6682596lo-hi-lo 330033 CH.16_ps gi|6682596 lo-hi-lo 326816 CH.20_hs gi|6552458lo-hi-lo 337603 CH22_C20H12.GENSCAN.16-2 lo-hi-lo 338561 CH22_EM:AC005500.GENSCAN.421-5 lo-hi-lo 338562 CH22_EM: AC005500.GENSCAN.421-6lo-hi-lo 333743 CH22_FGENES.264_1 lo-hi-lo 333845 CH22_FGENES.290_3lo-hi-lo 333849 CH22_FGENES.290_8 lo-hi-lo 334221 CH22_FGENES.360_1lo-hi-lo 334222 CH22_FGENES.360_3 lo-hi-lo 334578 CH22_FGENES.406_1lo-hi-lo 336662 CH22_FGENES.41-1 lo-hi-lo 336684 CH22_FGENES.46-1lo-hi-lo 335289 CH22_FGENES.527_2 lo-hi-lo 335290 CH22_FGENES.527_3lo-hi-lo 335293 CH22_FGENES.527_6 lo-hi-lo 337182 CH22_FGENES.570-2lo-hi-lo 335809 CH22_FGENES.617_6 (same as BFH4) lo-hi-lo 335810CH22_FGENES.617_7 lo-hi-lo 335824 CH22_FGENES.619_11 (same as BFH5)lo-hi-lo 336054 CH22_FGENES.683_3 lo-hi-lo 333124 CH22_FGENES.81_8lo-hi-lo 332340 AP000692 Hs.129781 chromosome 21 open reading frame 5lo-hi-lo 130380 AI949359 Hs.143600 type II Golgi membrane proteinlo-hi-lo 102962 R50032 Hs.159263 collagen, type VI, alpha 2 lo-hi-lo331306 AF102546 Hs.63931 dachshund (Drosophila) homolog lo-hi-lo 319408AA448090 Hs.87359 ESTs, Highly similar to RB18 MOUSE RAS-R lo-hi-lo312197 T96203 gb: ye48b07.r1 Soares fetal liver spleen lo-hi-lo 312405AI523875 gb: tg97d04.x1 NCI_CGAP_CLL1 Homo sapiens lo-hi-lo 312939AA495930 Hs.24444 Homo sapiens cDNA: FLJ22165 fis, clone H lo-hi-lo313475 AA010200 Hs.175551 ESTs lo-hi-lo 313624 AA525775 Hs.292523 ESTslo-hi-lo 316897 AA838114 Hs.221612 ESTs lo-hi-lo 317850 AI681545Hs.152982 hypothetical protein FLJ13117 lo-hi-lo 318541 T30290 Hs.107515ESTs lo-hi-lo 321325 AB033100 Hs.300646 KIAA protein (similar to mousepaladin) lo-hi-lo 321696 AA628791 Hs.76228 amplified in osteosarcomalo-hi-lo 322189 H65014 gb: yu66f10.r1 Weizmann Olfactory Epithello-hi-lo 322463 AI242754 Hs.137306 ESTs lo-hi-lo 322540 R76593 gb:yi60c11.r1 Soares placenta Nb2HP Homo lo-hi-lo 323131 AK002088 Hs.270124Homo sapiens cDNA FLJ11226 fis, clone PL lo-hi-lo 323243 W47525Hs.110771 Homo sapiens cDNA: FLJ21904 fis, clone H lo-hi-lo 323591AA301270 gb: EST14192 Testis tumor Homo sapiens cD lo-hi-lo 323753AK002161 Hs.70266 yeast Sec31p homolog lo-hi-lo 323835 AL042005 Hs.1117tripeptidyl peptidase II lo-hi-lo 323926 AA354572 gb: EST62857 JurkatT-cells V Homo sapien lo-hi-lo 324047 AI433357 *Hs.271340 ESTs lo-hi-lo324330 AA884766 gb: am20a10.s1 Soares_NFL_T_GBC_S1 Homo s lo-hi-lo324753 AA612626 Hs.144871 Homo sapiens cDNA FLJ13752 fis, clone PLlo-hi-lo 300702 AA075481 Hs.111334 ferritin, light polypeptide lo-hi-lo301712 BE083080 Hs.274323 Homo sapiens, Similar to sialyltransferalo-hi-lo 302380 AA325633 Hs.136102 KIAA0853 protein lo-hi-lo 302970W05608 Hs.312679 EST lo-hi-lo 303187 AA115962 Hs.323423 ESTs, Moderatelysimilar to B Chain B, lo-hi-lo 303194 AA082000 gb: zn26f07.r1 Stratageneneuroepithelium lo-hi-lo 305612 AA782347 Hs.272572 hemoglobin, alpha 2lo-hi-lo 304263 AA062837 gb: zm05b11.s1 Stratagene corneal stromalo-hi-lo 304275 AA070605 gb: zm53h09.s1 Stratagene fibroblast (937lo-hi-lo 304309 AA112147 gb: zm64c06.s1 Stratagene fibroblast (937lo-hi-lo 305503 AA759177 Hs.298148 ESTs, Weakly similar to KIAA0565protei lo-hi-lo 308615 AK000142 Hs.101774 hypothetical protein FLJ23045lo-hi-lo 309390 AW080585 gb: xc33f09.x1 NCI_CGAP_Co18 Homo sapienslo-hi-lo 104667 AI239923 Hs.30098 ESTs lo-hi-lo 310014 D60745 Hs.25925Homo sapiens clone 23860 mRNA sequence lo-hi-lo 318814 W07361 Hs.22545Homo sapiens cDNA FLJ12935 fis, clone NT lo-hi-lo 321896 C04863 Hs.47191ESTs lo-hi-lo 331661 W52448 Hs.56147 ESTs lo-hi-lo 332120 AA609684Hs.112748 Homo sapiens cDNA; FLJ21543 fis, clone C lo-hi-lo 332256AW975028 Hs.102754 ESTs lo-hi-lo 107252 D60745 Hs.25925 Homo sapiensclone 23860 mRNA sequence lo-hi-lo 112068 AI264847 Hs.22545 Homo sapienscDNA FLJ129356 fis, clone NT lo-hi-lo 117929 N51075 Hs.47191 ESTslo-hi-lo 119637 W52448 Hs.56147 ESTs lo-hi-lo 123712 AA609684 Hs.112748Homo sapiens cDNA; FLJ21543 fis, clone C lo-hi-lo 124560 AW975028Hs.102754 ESTs lo-hi-lo 105039 AA907305 Hs.36475 ESTs lo-hi-lo 105271AA807881 Hs.25329 ESTs lo-hi-lo 106689 AW296584 Hs.293782 ESTs lo-hi-lo106849 AL137281 Hs.17110 Homo sapiens mRNA; cDNA DKFZp434C2016 (flo-hi-lo 107071 AW385224 Hs.35198 ectonucleotidepyrophosphatase/phosphodi lo-hi-lo 108218 W57550 Hs.301526 hypotheticalprotein FLJ13181 lo-hi-lo 110930 BE242691 Hs.14947 ESTs, Weakly similarto ALU1_HUMAN ALU S lo-hi-lo 112098 R44714 Hs.106795 Homo sapiens cDNAFLJ13136 fis, clone NT lo-hi-lo 112170 BE246743 Hs.288529 hypotheticalprotein FLJ22635 lo-hi-lo 112902 AL035633 Hs.129190 Human DNA sequencefrom clone RP5-1046G1 lo-hi-lo 114877 AW024162 Hs.205125 ESTs lo-hi-lo116312 BE379794 Hs.65403 hypothetical protein lo-hi-lo 116739 H01463Hs.93534 ESTs lo-hi-lo 119267 AA064970 Hs.118145 ESTs lo-hi-lo 120570AA280679 Hs.271445 ESTs, Weakly similar to ALU1_HUMAN ALU lo-hi-lo121176 AL121523 Hs.97774 ESTs lo-hi-lo 123360 AA532718 Hs.178604 ESTslo-hi-lo 123974 NM_015678 Hs.3821 neurobeachin lo-hi-lo 124777 R41933gb: yg04f09.s1 Soares infant brain 1NIB H lo-hi-lo 128046 AA873285 gb:oh68h05.s1 NCI_CGAP_Kid5 Homo sapiens lo-hi-lo 128666 AA808466 Hs.103395hypothetical protein FLJ14146 lo-hi-lo 130639 AI557212 *Hs.17132 ESTslo-hi-lo 130693 R68537 Hs.17962 ESTs lo-hi-lo 131756 AA443966 Hs.31595ESTs lo-hi-lo 131985 AA503020 Hs.36563 hypothetical protein FLJ22418lo-hi-lo 132932 AW118826 Hs.6093 Homo sapiens cDNA: FLJ22783 fis, cloneK lo-hi-lo 134696 BE326276 *Hs.8861 ESTs lo-hi-lo 300967 AA565209Hs.269439 ESTs lo-hi-lo 301182 AW291411 Hs.192531 ESTs, Weakly similarto S00754 zinc fing lo-hi-lo 302595 AI699372 Hs.193247 Homo sapiensmRNA; cDNA DKFZp434A171 (fr lo-hi-lo 303132 AI929819 Hs.4055 chromosome21 open reading frame 50 lo-hi-lo 303506 AA340605 Hs.105887 ESTs, Weaklysimilar to Homolog of rat Z lo-hi-lo 303654 BE246743 Hs.288529hypothetical protein FLJ22635 lo-hi-lo 310026 AA278233 Hs.100691 ESTslo-hi-lo 310056 AI253072 Hs.145383 ESTs lo-hi-lo 310353 AI261700Hs.145544 ESTs lo-hi-lo 310371 AI262584 Hs.145575 ESTs lo-hi-lo 310430AI670843 Hs.200257 ESTs lo-hi-lo 310438 AW022192 Hs.200197 ESTs lo-hi-lo310455 AI277603 Hs.145990 ESTs lo-hi-lo 310787 AW262580 Hs.147674KIAA1621 protein lo-hi-lo 311067 AI587332 Hs.209115 ESTs lo-hi-lo 311422F00677 Hs.101316 ESTs lo-hi-lo 311465 AI758660 Hs.206132 ESTs lo-hi-lo312073 AA682393 *Hs.119237 ESTs lo-hi-lo 312105 T81819 Hs.302251 ESTslo-hi-lo 312108 T82331 *Hs.127453 ESTs lo-hi-lo 312292 AW450103Hs.151124 ESTs lo-hi-lo 312313 AW293341 Hs.122505 ESTs, Weakly similarto I38022 hypotheti lo-hi-lo 312600 AW970985 Hs.290853 ESTs lo-hi-lo312800 AI248774 Hs.126707 hypothetical protein FLJ11457 lo-hi-lo 312821AA699325 Hs.269880 ESTs lo-hi-lo 313097 AI676164 Hs.204339 ESTs lo-hi-lo313166 AI801098 Hs.151500 ESTs lo-hi-lo 313179 AA927670 Hs.131704 ESTslo-hi-lo 313280 AW960454 Hs.222830 ESTs lo-hi-lo 313689 AI608810Hs.193288 ESTs lo-hi-lo 314146 AI827237 Hs.282884 ESTs lo-hi-lo 314305AI280112 Hs.125232 Homo sapiens cDNA FLJ13266 fis, clone OV lo-hi-lo314456 AI867931 Hs.164595 ESTs lo-hi-lo 314465 AA602917 Hs.156974 ESTslo-hi-lo 314881 AI095087 Hs.152299 ESTs, Moderately similar toALU5_HUMAN A lo-hi-lo 314916 AA548906 Hs.122244 ESTs lo-hi-lo 315043AA806538 Hs.130732 KIAA1575 protein lo-hi-lo 315074 AA828284 Hs.136729Home sapiens cDNA: FLJ21348 fis, clone C lo-hi-lo 315214 AI915927Hs.34771 ESTs lo-hi-lo 315344 AW292176 Hs.245834 ESTs lo-hi-lo 315353AI373949 Hs.279610 hypothetical protein FLJ10493 lo-hi-lo 315439 T78413Hs.293696 ESTs lo-hi-lo 315528 R37257 Hs.184780 ESTs lo-hi-lo 315720AA292998 Hs.163900 ESTs lo-hi-lo 315772 AW515373 Hs.271249 Homo sapienscDNA: FLJ13580 fis, clone PL lo-hi-lo 315841 AW136397 Hs.247572 ESTslo-hi-lo 316042 AI469960 Hs.170698 ESTs lo-hi-lo 316244 AI640761Hs.224988 ESTs lo-hi-lo 316345 AW139408 Hs.152940 ESTs lo-hi-lo 316625BE540690 Hs.122156 ESTs lo-hi-lo 316738 AA889055 Hs.123468 ESTs lo-hi-lo316868 AI660896 Hs.195602 ESTs lo-hi-lo 316905 AW138241 Hs.210846 ESTslo-hi-lo 317224 X73608 *Hs.93029 sparc/osteonectin, cwcv and kazal-liked lo-hi-lo 317275 AI860444 Hs.202108 ESTs lo-hi-lo 317404 AI806867Hs.126594 ESTs lo-hi-lo 317488 AW071851 Hs.130628 ESTs lo-hi-lo 317916AI565071 Hs.159983 ESTs lo-hi-lo 317939 AI986208 Hs.244760 ESTs lo-hi-lo318486 T23514 gb: seq3329 1-NIB Homo sapiens cDNA clone lo-hi-lo 319897N46574 Hs.43838 ESTs lo-hi-lo 320654 AI160015 Hs.118112 ESTs lo-hi-lo320697 N62937 Hs.269109 ESTs lo-hi-lo 320787 AW088363 Hs.24240 ESTslo-hi-lo 321023 AW294316 Hs.125608 ESTs lo-hi-lo 321899 AW972832Hs.29468 ESTs lo-hi-lo 322939 AA101697 Hs.211270 ESTs lo-hi-lo 323045AA148950 Hs.188836 ESTs lo-hi-lo 323091 AI902456 Hs.210761 ESTs lo-hi-lo323262 AL133990 Hs.190642 ESTs lo-hi-lo 323410 AW118683 Hs.154150 ESTslo-hi-lo 323645 AW445014 Hs.197746 ESTs lo-hi-lo 324598 AW972227Hs.163986 Homo sapiens cDNA: FLJ22765 fis, clone K lo-hi-lo 324666T78413 Hs.293696 ESTs lo-hi-lo 324674 AA541323 Hs.15831 ESTs lo-hi-lo324713 AI093930 *Hs.313466 ESTs lo-hi-lo 324790 AI334367 Hs.159337 ESTslo-hi-lo 324804 AI692552 gb: wd73f12x1 NCI_CGAP_Lu24 Home sapienslo-hi-lo 330728 AI905520 Hs.29672 ESTs lo-hi-lo 330760 H04588 Hs.30469ESTs lo-hi-lo 330776 AW953805 Hs.21887 ESTs lo-hi-lo 330824 AB037732Hs.61441 KIAA1311 protein lo-hi-lo 331028 AI539652 Hs.28338 KIAA1546protein lo-hi-lo 331046 N66563 Hs.191358 ESTs lo-hi-lo 331050 BE007967Hs.155795 ESTs lo-hi-lo 331053 AI949841 Hs.183146 ESTs, Moderatelysimilar to ALU1_HUMAN A lo-hi-lo 331180 R44692 Hs.6640 Human DNAsequence from PAC 75N13 on chr lo-hi-lo 331313 AA761094 *Hs.80618hypothetical protein lo-hi-lo 331337 N74392 Hs.50495 ESTs lo-hi-lo331393 AW976438 *Hs.17428 RBP1-like protein lo-hi-lo 331432 AA262451Hs.38485 ESTs lo-hi-lo 331517 AA765603 Hs.180877 H3 histone, family 3B(H3.3B) lo-hi-lo 331686 AW474960 Hs.182258 ESTs lo-hi-lo 332002 AI579909Hs.105104 ESTs lo-hi-lo 332043 AA371307 Hs.125056 ESTs lo-hi-lo 332265AW770320 Hs.222413 ESTs lo-hi-lo 332314 R41396 Hs.101774 hypotheticalprotein FLJ23045 lo-hi-lo 131517 AB037789 Hs.263395 sema domain,transmembrane domain (TM), lo-hi-lo 315352 AA604799 Hs.136528 ESTs,Moderately similar to ALU1_HUMAN A lo-hi-lo 315498 AA628539 Hs.116252ESTs, Moderately similar to ALU1_HUMAN A lo-hi-lo 321489 AI459177Hs.172759 ESts, Moderately similar to ALU7_HUMAN A lo-hi-lo 106099NM_012068 Hs.9754 activating transcription factor 5 lo-hi-lo 105726NM_012068 Hs.9754 activating transcription factor 5 lo-hi-lo 319926AI820719 Hs.154662 DnaJ (Hsp40) homolog, subfamily A, membe lo-hi-lo314915 AI673735 Hs.187748 ESTs, Weakly similar to ALU1_HUMAN ALU Slo-hi-lo 315198 AI741506 Hs.186753 ESTs, Weakly similar to ALU1_HUMANALU S lo-hi-lo 324302 AW972771 Hs.292471 ESTs, Weakly similar toALU1_HUMAN ALU S lo-hi-lo 331341 BE541042 *Hs.23240 Homo sapiens cDNAFLJ13496 fis, clone PL lo-hi-lo 113783 AL359588 Hs.7041 hypotheticalprotein DKFZp762B226 lo-hi-lo 313552 AI889208 Hs.17283 hypotheticalprotein FLJ10890 lo-hi-lo 103989 AA315993 Hs.105484 Homo sapiensregenerating gene type IV m lo-hi-lo 331492 AK001114 Hs.53913hypothetical protein FLJ10252 lo-hi-lo 110837 H03109 Hs.108920 HT018protein lo-hi-lo 330814 AI955040 Hs.265398 ESTs, Weakly similar totransformation-r lo-hi-lo 312226 AA315703 Hs.199993 ESTs lo-hi-lo 102034AI903474 Hs.230 fibromodulin lo-hi-lo 134671 BE263255 Hs.302749FK506-binding protein 9 (63 kD) lo-hi-lo 131083 Y09763 Hs.22785gamma-aminobutyric acid (GABA) A recepto lo-hi-lo 309575 AW168096Hs.169476 glyceraldehyde-3-phosphate dehydrogenase lo-hi-lo 134332D86962 Hs.81875 growth factor receptor-bound protein 10 lo-hi-lo 132904NM_005518 Hs.59889 3-hydroxy-3-methylglutaryl-Coenzyme A sy lo-hi-lo302910 N77976 Hs.251577 hemoglobin, alpha 1 lo-hi-lo 133731 N71725*Hs.272572 hemoglobin, alpha 2 lo-hi-lo 303297 AF070623 Hs.13423 Homosapiens clone 24468 mRNA sequence lo-hi-lo 108732 AA258888 Hs.107476 ATPsynthase, H+ transporting, mitochond lo-hi-lo 108731 AA258888 Hs.107476ATP synthase, H+ transporting, mitochond lo-hi-lo 302123 AB013452Hs.144931 ATPase, aminophospholipid transporter (A lo-hi-lo 131614AB002438 Hs.29596 Homo sapiens mRNA from chromosome 5q21-2 lo-hi-lo104933 N94126 Hs.12969 hypothetical protein lo-hi-lo 302235 AL049987Hs.166361 Homo sapiens mRNA; cDNA DKFZp564F112 (ft lo-hi-lo 320574AL049443 Hs.161283 Homo sapiens mRNA; cDNA DKFZp586N2020 (f lo-hi-lo324678 AI990739 Hs.77868 ORF lo-hi-lo 331022 H03109 Hs.108920 HT018protein lo-hi-lo 332430 H25350 Hs.21145 hypothetical protein FLJ22489lo-hi-lo 330601 U90916 Hs.82845 Homo sapiens cDNA; FLJ21930 fis, clone Hlo-hi-lo 101988 AF221521 Hs.8068 hematopoietic PBX-interacting proteinlo-hi-lo 102859 AL036058 *Hs.76807 major histocompatibility complex,class lo-hi-lo 101363 M11321 lo-hi-lo 133968 AA355986 Hs.232068transcription factor 8 (represses interl lo-hi-lo 332530 M31669 Hs.1735inhibin, beta B (activin AB beta polypep lo-hi-lo 317777 NM_014785Hs.47313 KIAA0258 gene product lo-hi-lo 100452 D87742 Hs.241552 KIAA0268protein lo-hi-lo 112988 NM_014867 Hs.5333 KIAA0711 gene product lo-hi-lo320848 AB020691 Hs.198232 KIAA0884 protein lo-hi-lo 105162 AL133033*Hs.4084 KIAA1025 protein lo-hi-lo 133905 AB028974 Hs.137476 KIAA1051protein lo-hi-lo 331406 BE176893 Hs.23440 KIAA1105 protein lo-hi-lo321441 AF107493 Hs.118498 Homo sapiens LUCA-15 protein mRNA, spliclo-hi-lo 131913 AW207440 Hs.185973 degenerative spermatocyte (homologDroso lo-hi-lo 135424 U67611 transaldolase 1 lo-hi-lo 128506 L40904Hs.100724 peroxisome proliferative activated recep lo-hi-lo 330506AI130740 Hs.6241 phosphoinositide-3-kinase, regulatory su lo-hi-lo311251 AI655662 Hs.197698 ESTs lo-hi-lo 314171 AI821895 Hs.193481 ESTslo-hi-lo 106096 AW379378 Hs.170121 protein tyrosine phosphatase,receptor t lo-hi-lo 133740 AW162919 *Hs.170160 RAB2, member RAS oncogenefamily-like lo-hi-lo 119521 W38038 lo-hi-lo 119546 W38169 lo-hi-lo119559 W38197 lo-hi-lo 133797 AL133921 Hs.76272 retinoblastoma-bindingprotein 2 lo-hi-lo 305097 AA642964 Hs.163593 ribosomal protein L18alo-hi-lo 120256 AA169801 Hs.98710 hypothetical protein lo-hi-lo 322919AA178955 Hs.271439 ESTs lo-hi-lo 300566 R34926 Hs.326392 son ofsevenless (Drosophila) homolog 1 lo-hi-lo 330694 AI741617 Hs.108447spinocerebellar ataxia 7 (olivopontocere lo-hi-lo 302416 AL120259Hs.76691 stannin lo-hi-lo 319289 AA037534 Hs.79059 transforming growthfactor, beta recepto lo-hi-lo 134656 AI750878 Hs.87409 thrombospondin 1lo-hi-lo 130117 U06641 Hs.150207 UDP glycosyltransferase 2 family,polype lo-hi-lo 124357 N22401 gb: yw37g07.s1 Morton Fetal Cochlea Homelo-hi-lo 108293 AA069155 gb: zm10f11.s1 Stratagene pancreas (93720lo-hi-lo 108657 BE567753 Hs.132955 BCL2/adenovirus E1B 19 kD-interactingpro lo-hi-lo 108658 AA641695 gb: nr62h10.s1 NCI_CGAP_Lym3 Homo sapienslo-hi-lo 331278 AA071383 gb: zm61d05.r1 Stratagene fibroblast (937lo-hi-lo 108340 AA069820 Hs.180909 peroxiredoxin 1 lo-hi-lo 108679AA115963 Hs.323423 ESTs, Moderately similar to B Chain B, lo-hi-lo108406 AA075424 Hs.325505 ESTs, Moderately similar to HBA_HUMAN HElo-hi-lo 114598 AA075601 gb: zm88c05.r1 Stratagene ovarian cancerlo-hi-lo 108462 AA079347 gb: zm96c06.s1 Stratagene colon HT29 (937lo-hi-lo 108466 AA079409 gb: zm96h02.s1 Stratagene colon HT29 (937lo-hi-lo 108489 AA082977 gb: zn07h10.r1 Stratagene hNT neuron (937lo-hi-lo 330859 AA082977 gb: zn07h10.r1 Stratagene hNT neuron (937lo-hi-lo 108505 AA083376 gb: zn09g08.s1 Stratagene hNT neuron (937lo-hi-lo 331283 AA467736 Hs.275437 ESTs lo-hi-lo 100641 AW068302*Hs.182183 Homo sapiens mRNA for caldesmon, 3′ UTR lo-hi-lo-hi 100642AW068302 *Hs.182183 Homo sapiens mRNA for caldesmon, 3′ UTR lo-hi-lo-hi325889 CH.16_hs gi|5867087 lo-hi-lo-hi 338038 CH22_EM:AC005500.GENSCAN.149-9 lo-hi-lo-hi 338316 CH22_EM:AC005500.GENSCAN.304-2 lo-hi-lo-hi 100999 H38765 Hs.80706 diaphorase(NADH/NADPH) (cytochrome b-5 lo-hi-lo-hi 331131 R54797 gb: yg87b07.s1Soares infant brain 1NIB H lo-hi-lo-hi 310955 AI476732 Hs.263912 ESTslo-hi-lo-hi 311137 AW207582 Hs.196042 ESTs lo-hi-lo-hi 311598 AW023595Hs.232048 ESTs lo-hi-lo-hi 313070 AI422023 Hs.161338 ESTs lo-hi-lo-hi110844 AI740792 Hs.167531 methylcrotonoyl-Coenzyme A carboxylase 2lo-hi-lo-hi 120328 AA923278 Hs.290905 ESTs, Weakly similar to protease[H. sapi lo-hi-lo-hi 105914 AW245680 Hs.9701 growth arrest andDNA-damage-inducible, lo-hi-lo-hi 129389 NM_012445 *Hs.288126 spondin 2,extracellular matrix protein lo-hi-lo-hi 102759 NM_005100 Hs.788 Akinase (PRKA) anchor protein (gravin) lo-lo-hi 100168 H73444 Hs.394adrenomedullin lo-lo-hi 102348 U37519 Hs.87539 aldehyde dehydrogenase 8lo-lo-hi 134158 U15174 Hs.79428 BCL2/adenovirus E1B 19 kD-interactingpro lo-lo-hi 133908 AU076820 Hs.325474 caldesmon 1 lo-lo-hi 101883AU076743 Hs.75613 CD36 antigen (collagen type I receptor, lo-lo-hi327821 CH.05_hs gi|5867968 lo-lo-hi 134133 AA262294 Hs.180383 dualspacificity phosphatase 6 lo-lo-hi 103000 NM_001975 *Hs.146580 enolase2, (gamma, neuronal) lo-lo-hi 109251 AA194776 Hs.85935 EST lo-lo-hi315566 AB037810 Hs.18760 KIAA1389 protein lo-lo-hi 324697 AK000742Hs.126774 L2DTL protein lo-lo-hi 306011 AA896986 gb: at06a08.s1 Barsteadspleen HPLRB2 Hom lo-lo-hi 307111 AI174528 gb: an45g10.s1 Gessler Wilmstumor Homo s lo-lo-hi 106639 AV655272 Hs.20252 novel Ras family proteinlo-lo-hi 106753 AI656166 Hs.7331 hypothetical protein FLJ22316 lo-lo-hi107974 AW956103 Hs.61712 pyruvate dehydrogenase kinase, isoenzymelo-lo-hi 112033 R49031 Hs.22627 ESTs lo-lo-hi 113816 H46008 Hs.31518ESTs lo-lo-hi 116024 AA088767 *Hs.83883 transmembrane, prostate androgeninduced lo-lo-hi 116158 AA381807 Hs.61762 hypoxia-inducible protein 2lo-lo-hi 119071 R31180 gb: yh62b02.s1 Soares placenta Nb2HP Homolo-lo-hi 120132 W57554 Hs.125019 ESTs lo-lo-hi 120655 AA305599 Hs.238205hypothetical protein PRO2013 lo-lo-hi 122411 AW172356 Hs.99083 ESTslo-lo-hi 320779 AA815354 Hs.169898 ESTs lo-lo-hi 321024 AW246216Hs.32058 Homo sapiens C1orf19 mRNA, partial cds lo-lo-hi 321408 AW081530Hs.137088 ESTs, Weakly similar to ALU1_HUMAN ALU S lo-lo-hi 323620AA306997 Hs.268362 ESTs, Weakly similar to hypothetical pro lo-lo-hi314946 AI097229 Hs.217484 ESTs lo-lo-hi 320683 AA334511 Hs.26638 ESTs,Weakly similar to unnamed protein lo-lo-hi 128959 AI580127 Hs.107381hypothetical protein FLJ11200 lo-lo-hi 128896 T53925 Hs.107fibrinogen-like 1 lo-lo-hi 133592 AV652066 Hs.75113 generaltranscription factor IIIA lo-lo-hi 103245 BE566343 *Hs.28988glutaredoxin (thioltransferase) lo-lo-hi 314785 AI538226 Hs.32976guanine nucleotide binding protein 4 lo-lo-hi 103677 Z83806 gb: H.sapiens mRNA for axonemal dynein he lo-lo-hi 131170 NM_014253 *Hs.23796odz (odd Oz/ten-m, Drosophila) homolog 1 lo-lo-hi 131164 AW013807Hs.182265 keratin 19 lo-lo-hi 100409 D86957 Hs.80712 KIAA0202 proteinlo-lo-hi 133167 AW162840 Hs.6641 kinesin family member 5C lo-lo-hi319080 AW967646 Hs.23023 ESTs lo-lo-hi 330706 AF097994 Hs.301528L-kynurenine/alpha-aminoadipate aminotra lo-lo-hi 104052 NM_002407Hs.97644 mammaglobin 2 lo-lo-hi 100547 M57417 gb: Homo sapiens mucin(mucin) mRNA, part lo-lo-hi 103145 X66276 Hs.169849 myosin-bindingprotein C, slow-type lo-lo-hi 301015 AV655272 Hs.20252 novel Ras familyprotein lo-lo-hi 311013 AA224760 *Hs.153 ribosomal protein L7 lo-lo-hi132050 AI267615 Hs.38022 ESTs lo-lo-hi 132349 AW975654 *Hs.181286 serineprotease inhibitor, Kazal type 1 lo-lo-hi 130889 AW972512 Hs.20985sin3-associated polypeptide, 30 kD lo-lo-hi 130791 AF030403 Hs.199263Ste-20 related kinase lo-lo-hi 130385 AW067800 Hs.155223 stanniocalcin 2lo-lo-hi 127229 AA316181 Hs.61635 six transmembrane epithelial antigenof lo-lo-hi 133820 S69681 *Hs.177582 surfactant, pulmonary-associatedprotein lo-lo-hi 129523 M13231 Hs.274509 T cell receptor gamma constant2 lo-lo-hi 321415 BE621807 Hs.3337 transmembrane 4 superfamily member 1lo-lo-hi 131859 AW960564 *Hs.3337 transmembrane 4 superfamily member 1lo-lo-hi 133444 M63978 Hs.73793 vascular endothelial growth factorlo-lo-hi 332567 AW939251 *Hs.25647 v-fos FBJ murine osteosarcoma viralonco lo-lo-hi 131328 AW939251 *Hs.25647 v-fos FBJ murine osteosarcomaviral onco lo-lo-hi 315901 AI521558 Hs.7331 hypothetical proteinFLJ22316 lo-lo-hi 104394 AA129551 Hs.172129 Homo sapiens cDNA: FLJ21409fis, clone C lo-lo-hi 103739 AA115173 gb: zn30d02.s1 Stratageneneuroepithelium lo-lo-hi 103797 AA080912 gb: zn04d03.r1 Stratgene hNTneuron (937 lo-lo-hi 103804 AA129196 gb: zn29d08.r1 Stratgeneneuroepithelium lo-lo-hi

TABLE 1B Pkey CAT Number Accessions 108462 116651_1 AA079347 AA079506AA079538 AA079442 108489 118662_1 AA082977 AA082955 AA082956 10121617379_1 AA284166 AA314707 L25876 L27711 AA092745 N92087 U02681 AA315766BE385121 AA352693 NM_005192 AI739135 AI066521 AW173105 AA257103 AA450169AW261971 AA305065 AI954494 AW950384 AW732122 AA830348 AA789097 AA777794AA284072 BE564465 AI005313 AA804528 AI041134 AI700317 AI352491 AA856987AA769007 AA494334 AA769862 AA831168 AI143496 BE090796 AA831166 AI141222AI372907 N64843 AI075136 AI076701 AA464156 AI076409 AI273523 AA627383BE043332 T96666 AA158102 AA158059 AW340182 AA257019 AI206700 AI678081AA757304 AA055005 AW059834 AL039012 131328 8509_1 AW939251 NM_005252AU076596 V01512 V01512 AW579056 AA249247 AI590359 AW510478 AW518282BE046054 AW874080 AI268596 AA996237 AI695592 AI244117 AA290764 AA401957AA505878 AA428304 W74018 W74016 AA040944 AI272071 AA745909 AA620979AA019816 AI245094 AW009706 AA662536 AW024264 AI268601 AA932024 AW513222AW024169 AI659705 AA932526 AA975329 AI567603 AI889320 AA514238 AA020837AI623966 AA843677 AA477453 AA496353 AW372625 AV656426 K00650 W96348N62388 R95977 AA434270 AI093633 T27639 AW960245 AW881177 R15253 N36936F07701 AA319315 AA337290 AA284642 AA344052 F05184 AA351062 AA378451AW794233 AW884380 N36951 R49879 AB022276 AA300350 AW839435 AW191708BE220350 AA280404 AA485546 AW794235 AV654223 AW838891 AA295986 N72823AA335648 AA371089 AW845414 H63166 R12840 AA379680 AA477579 R13148 H71003H71015 AA362156 AW750674 AW845415 AA366924 AW608044 AI570388 R31511R33906 R33921 AW663022 AW360985 AI207838 AW607239 AI672451 AI573282AW794752 AA370328 AW998896 AW797239 AW998912 AW794742 AI954543 AI810067AW073373 AA370325 AW195330 C18106 AW998736 R79476 AA429721 AI891081AI381534 AW022137 AW020000 AI630329 N99428 AI870222 AI971257 AI922196AI857753 AW579397 D56749 AI925005 AI685727 AW805573 AI982678 AI784604AI005625 AW877772 AI634947 AI950829 AA493243 BE166086 AI801820 AI925643AI627992 AW316704 AI261318 D57757 AA887178 AW770406 AI972075 AI222254AI675794 D58060 AI701954 D58166 AI799500 AW805669 AW276098 AW874253AI962991 AI248184 AW996924 AI017462 AW022260 AI885957 BE176841 AA878863AI697419 AW662094 AI479529 BE177025 D57403 AA507952 AW664593 AW800998AI985773 AA566089 AA442759 AI624670 AI460284 AI800205 AI537788 AI537593AI244382 AA583463 AA922678 AA864382 AI610837 D58070 AA844283 AA947992N73801 AI453821 D58184 AI678887 AW243755 AA746085 D57742 AA757380 R44148AA496403 BE180303 AW363528 BE006616 D57395 AW805507 AW805511 AA617991AI373585 H30122 D57744 AW805501 D57691 D58148 AW873164 AW768483 D57601AA777812 AA837997 BE180123 D57599 AA485387 AW022208 D58096 N67917 W95944AW805506 D57518 D57990 AI074096 D56521 D58151 AA428720 D56648 D57778AW805504 D57750 D58108 AW021706 D57449 D57041 D58277 D56935 AI356974D57023 AA018712 H27631 D57851 D57514 D57268 D57468 AW805646 AI278945D57323 D56986 D57539 D57829 D58078 AW805515 AI348684 D57772 R74449BE041558 D56746 AW798485 D56640 AA985597 D56702 D56849 D56874 AW581419AA470397 D57591 AW798984 T27640 N66497 D56803 AA618186 AW805647 D57945N23726 D56637 N23730 D56992 BE176882 BE176839 BE176909 D56757 N68137D56987 AI559806 AA631437 D57464 D56718 C17030 T29278 D57377 AW021936AW118330 AA515358 D56610 AA494092 D56934 T97774 AI473546 R74350 R84834AA579200 D56616 C03207 D57391 N52416 D56928 R79209 D56925 AA020879D45546 AI858769 R20750 T09381 F01435 AW627906 D58202 AI933993 F01912H27552 AA174191 T16515 AW023216 AA434146 H83387 AI346751 V01512 V01512AA576407 AW365140 AA937471 BE174681 AI568829 AI274663 R85530 AL048225H83388 AW798734 124148 31218_1 BE300094 BE384439 AW794648 NM_002305M57678 AI929016 AU076727 Z83844 Z83844 AI906100 W44519 H98497 AA188069AA572687 AA035793 W93978 BE409220 AA359751 AA502475 H28319 AA527889AA432335 AA864762 AA340061 C05180 W68192 AA327811 AA345871 AI750205N34093 N86639 AA085753 AA603415 AI355561 AA442262 N42135 C04367 N57266AI038364 AI184846 AI928853 X15256 J04456 AA603552 AA317300 AA588615AA813495 N40276 AA400624 AW264898 H21418 AA643822 AA603569 AA507955N44497 AI000869 AW079049 AA614629 AA303987 AA362817 H54502 N85495 W52256F30575 AA568129 H26935 W93977 AA373651 AA872398 AI332540 AW572787 F20782AA442263 AW301076 AA558556 AA825366 W23842 AI038829 AA302408 AA374629AA614477 AA341686 AA374846 AA187091 F24764 AA157099 AA374853 AA991592F26839 AA744090 AA936881 AA374627 AA329755 AA854398 AA618108 AA973600AA757956 W44520 AA379779 AA373698 AA369135 AA380039 BE408327 AA375117AA375744 AA380014 AA373556 AI335987 AA903267 AA828223 F25088 AI246573AA299386 BE275844 BE275666 BE384214 BE620707 AA975886 AA858048 BE548468AA193055 BE274324 AI870164 AA129614 AA922761 AA935745 AA374567 AI580916AA374661 AW239224 AA374466 N52172 F24306 AA300453 AA363443 AA588627F19159 AA580021 N90877 AA654335 AA679168 AA573071 AW238834 AA988739AW239423 AA976330 AI074239 AA999911 AI200930 AI971173 AI187321 AA937760AI016242 AA373684 AI094874 AI302174 AA641237 AI370974 AI971010 AA400379AA679137 AI096579 AI001918 AA524101 X14829 AA081302 N30374 AI338782W74444 AA528232 AI734954 AW188024 AA433857 W92348 W94431 AI708356AI753458 AA494460 AA825257 AA614246 AA039477 AI350213 AI309110 AA745965AA291936 AW001376 AI066764 W74407 F30627 AA291937 AA480615 AA931667AA331315 AI936154 AA824332 AA181109 AI017291 AA934736 AA062637 AA599977H54814 AA635624 AI802655 AA564078 R69997 AA716551 F30469 AA961030AI126757 AI183943 AI066798 AI419436 AA302095 AA157768 AA953030 AA588476AA131216 T79619 AI752885 AA614820 AA988962 AI143561 AA493182 AI302481AA301613 R73520 AA069898 AA374944 AW364221 AA342013 AI244949 F36390AW050980 N79486 AA101160 T68112 AI750204 AA328787 H02617 AA314734AA527923 AA307835 AI885112 AI872905 AA534666 AA188363 AI192490 H45772AI824700 AI184276 AW079473 N29847 AA720843 AA720914 AA573391 H54416T59424 AI824457 AA304220 AA482553 W72882 AA627932 H27514 H28400 W68050H20953 AA635786 H21376 AA514046 AI342823 F29905 H25999 AA757144 H21636F22104 AA428650 F27143 F28346 AA535690 H45771 AA548851 AW170154 H45646W92274 AI921614 AA176461 AW170153 AI927284 AI161206 AA594439 T28595H41129 AI497579 AA978015 AA328875 AA373653 AA090973 AA328623 AA328759AA366468 AA375406 H46976 R86050 H02722 AA328321 AA328205 R62358 AA373717AA304138 AA304224 AA301603 H54867 AA374783 AA376232 AA373239 AA374917AA375673 AA303857 AA376466 AA376461 AA302613 AA304082 AA301731 AA357988AA303328 R25744 AA301587 N78746 H20508 AA659423 R47960 AA825456 AI001806AI245114 AA729223 AA860271 AI913845 H26296 AA733035 AA340965 AA304291H27356 H20598 AA129613 R69996 AA157689 H20992 W16630 W16561 H25964H21754 W01159 W42885 AA176730 H39504 N39788 AA182956 H27585 AA082164AA328927 AA339934 H61805 H61804 H45580 AA476229 AA714104 AA507471AI262184 AI139474 AI139476 AI001045 AA614374 AA593153 F33347 F34679T68225 N25703 AA186999 AI623318 F18313 N72069 AA903161 H38546 H28672AI880529 AI128960 AA299183 AW768886 F17445 F30433 AA303984 AA303687AA309366 H28320 AI659479 AA627222 AA064882 AA507447 R53171 AA039476T79704 R36589 T83222 H26453 AA298798 R53415 N84918 F37846 R94423AA352679 AA308615 AA375442 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AA490520 AA720591 AA236827 AA760777 AA515110 AI188075AA680139 AA677413 W93115 AA282549 AA249038 331336 genbank_AA287450AA287450 331337 169430_1 N74392 N74444 AA287662 AA205513 AA287862 W02641W03156 331341 172787_1 BE541042 AW069774 AW664160 AW189935 R27296AI872737 H04753 R67040 AA687583 R78627 AA214158 W02221 AA303125 AI865269R46578 AI571977 331353 191360_2 AA953006 AI276403 AI277578 AA256327AA406577 AA479917 331363 18581_1 AW582256 AW956284 AF038451 NM_006408AA316115 AA315629 AW369360 AA314225 AF007791 AA421527 BE072059 AI817063AW194118 AW192785 AI075324 AA298537 AI634717 AI380637 AW151674 AI888294AW190856 AW364247 AI080640 AW152548 AW002338 AW614754 AI445913 AI828325AA573742 AI436796 AA909945 AI735767 AW304001 AI475938 AW303846 AA582017BE076995 BE049240 AI678847 AW471069 AI720013 AW951790 AI888914 AW272720AI801054 AA582851 AW073291 AA583091 AA315049 AI828251 AI801784 AI805627AI025266 AA776960 AI559391 AI800431 AI800451 AA838499 AI378681 AA884931AI242802 AW769127 AI184843 AA316874 AA565996 AA442829 AA593818 AW027843AI249798 AI378390 AI277266 AA552670 AA970336 AI473626 AI275085 AA622524AI610106 AI291994 AI476691 AA838482 AI925030 AI146786 AI582452 AI537173AI040152 AI678427 AI469656 AI445130 AI916480 AI285429 AW602019 AI358508AA687567 AA421562 AA425142 AW190915 AA570785 AI888732 AA632103 AI924494AW152169 AI891014 AA565444 AW191880 AW591300 AA581848 AI473553 AI675714AA501945 AI685830 AI469613 AI933636 AI972701 AI972499 AI581525 AA526975AI623264 AA639696 AA513297 AI400863 AW080588 AA558986 AI926128 AI537212AI695291 AA327356 AA625485 AF088867 AA298527 T24475 AA476675 AA055880AA314206 AA315408 AA316508 AA307697 AW844413 AA314052 AW370274 AW582421AW364225 AI815198 AW166169 BE072073 AI675865 AA315613 AA426228 AA314146AA437001 AA307795 AA316233 AA314372 AA316967 AA315724 AA313235 AW369331AA244356 T86663 AW868072 331393 7091_1 AW976438 AF227899 AL079586AW242991 AA296993 AF083249 AA743290 AA082927 H38607 AA046204 AI458928AA810515 AI985329 AW450239 AA279595 AI632699 AI091806 BE221365 AI130893AA082926 AI017851 AI474175 AA669471 AA169631 AA248905 AL133594 H08612AA247824 AA399016 AI268687 AA479433 BE467082 AA961159 AW890022 AW890015AW899450 AW890140 AW890016 AI656542 AI656530 AI284462 AW590370 T61838AA478729 AA047401 N53320 AA834839 AW264473 AW007865 AA249450 AA167427AI365221 AI701000 AI680921 AA385375 AW954119 AI860823 C75362 AI492007AI539819 AW014989 AW628976 AI473662 AW276150 AA047467 N67246 H08613AI559629 AI811077 AI039475 AI431949 AA907555 AI915180 AW148492 AI242862AI365222 BE018520 AA412178 BE302119 AI823337 AA905198 N83376 AI382420AA776507 T94766 W67770 AW369401 AA262427 W84569 AW968527 R20183 AA485189F06553 BE080982 AW995604 BE080849 BE080826 BE080978 AA167428 BE080830AW995687 AA171673 AW995686 331406 8041_1 BE176893 BE176888 AA397686AI620405 AI299697 AI702708 AA987446 AI693106 AW889017 AA442537 AI922509AI653242 AW237517 AW418517 AA806072 AI968500 AI760938 AI537876 AI811401AW244033 AL046630 AI143522 AW263905 AI985159 AI962850 AI202886 AW300419AA251838 AA861778 AI025639 AA399033 AI924740 AI800259 AA179395 AA610064AI865176 AI289921 AA565722 AW770029 AW439544 AI025969 AW380171 AW080913AW749363 AA496833 R58228 H09840 AA836330 AA764813 AI352142 T31439 Z43462F08407 H47178 AI114660 N48131 AI061591 N48117 BE167338 AW384456 T19719R23036 AW384458 N38985 T19720 AA075344 AI671613 AW842474 BE550608AA778899 AA279243 AA496875 AI888310 AI088077 AI493142 AI338275 AW872997AI459760 AA909786 AI292044 AA136299 H09755 AA279929 AA279124 AI871819AI924804 N38971 AI000293 AW022179 AA952968 R22931 AI244527 AI003708Z39538 F04624 H47088 AF180425 W56074 AA287344 H96262 W19197 AA456123W38634 AA428762 AA485167 W24739 AW368029 AA236691 BE075101 AA136180AA075597 AI217101 R81770 AA410581 331432 193887_1 AA262451 AA760878H67704 AA748621 331442 48779_−2 H77381 331492 11196_1 AK001114 AI949698AI694727 BE501500 AI436121 AI769868 AI298375 AA026113 AA723068 F13681AA908961 AW821352 AA976618 AI814359 AW070254 AA933772 AW298059 AI829001AW515661 AI346450 AW664032 AA909492 AA961461 N34017 AW371083 AA918350AI346671 AI337550 T86138 AI128634 AI738898 AI738907 AA026199 AA089670331517 288032_1 AA765603 AI675581 AI355934 AW166822 AI566925 AA767454AA814384 AA730044 AW070292 N48610 AI341862 AI683402 AA424064 N23063N23090 N38898 AI627249 AW339549 AI281421 AA708329 AW976803 331661452840_1 W52448 W52773 AI201922 AA781389 AI651363 BE550487 AW236796AW304858 AI695978 AI220182 331686 1153509_1 AW474960 W88502 H70430W86162 331919 300127_1 AA446869 AI368257 BE550153 AI080424 AW590470AI478438 H46178 AW975073 AI701561 AW204114 BE165640 AA658113 AI214533AW206932 AW885560 AW607277 AA446983 R49782 332002 188158_1 AI579909AW967587 AA766314 AW173502 AA831027 AA991192 AW407403 AW299333 AI356937AA761270 AI979179 AW207045 AA482009 AW070877 AA280294 AW469832 AA250879AA251072 332043 262097_1 AA371307 AW968802 AA988769 AA642428 AA490831W96347 AA649036 332120 374423_1 AA609684 AA758732 332256 349165_1AW975028 AA551969 AA644028 AA689303 AI220334 AI220090 AI925480 N66393332265 1028361_1 AW770320 AW119114 D61961 N74375 N74427 332314 477192_1R41396 T25915 H23454 AA846250 H42125 D62549 H18484 C00804 AI446466AW206738 AI445643 T25862 AI339005 332340 22951_1 AP000692 NM_005128AJ237839 R82151 AB023150 AW410488 AJ003273 AW379450 AA322182 R82140AJ001857 BE004377 AW083855 AI096738 AW070676 AA678924 AW085802 W15495BE551040 AI699147 AI510780 R82143 R82122 332386 399_1 NM_000481 D14686D13811 AU076448 BE293629 BE305090 BE250035 AA341258 F11299 F07978AI129601 N85119 W79101 C18828 R09579 AW850108 N78273 AW950618 H79161BE008484 AI081517 AA534975 AI290815 AA741122 AA921395 AW591508 AI885347AI348172 N59532 W79815 AA947150 AW074248 AW751377 AI057053 AI346712AI193862 H85887 AA983969 AA804465 AA886299 AI217497 AI351816 F08959AA503087 AA993107 F04230 AA550742 AA962122 AA969722 AI625176 T28574AI767567 332397 35955_1 AB027249 AF237709 BE245643 AW403476 AB027250AF189722 AA353579 BE537775 W25389 AW962279 AW818197 AA449542 AA448898AW974523 AW195611 AI393315 AI738792 AW665895 AW574679 AA913471 AA651780AA737663 AI015407 AI366737 AI285359 BE245537 AA740847 AW513628 AI278471AA405512 AI955022 AI276896 AI932328 AA971676 AI002631 AW193686 AW118095AI969593 BE466775 AI375878 AI911763 AW269502 AA476576 AA768652 AI300231AI216689 AI287319 332430 53900_1 H25350 H28544 AI955873 N29952 N29938R12730 AA229527 H25302 AA854239 AW051288 AA598738 H62306 AI337901AI056386 T18606 H82372 AI761586 AI889010 AW043582 AI765252 AA620587AI190510 AI494128 AI161119 AI457908 AI420691 AW236132 AI917195 AI949791AI433283 AI146385 AI074325 H62210 AA846154 AI344715 AI982957 AA524256R39782 AI360821 AI124983 AA723581 AI289068 AW137304 AW073116 W37495AI335838 AL121074 AW264699 AA865259 AI089458 AA782578 AA788618 AA595002AI167549 W07131 AL120665 332530 2356_1 M31669 M31682 M13437 AW370612F00759 AI659282 W44452 AA600841 W44338 AA608807 AW973553 AW973542AA505620 AI458719 AA936480 AA973451 T29876 AA577032 AI874161 AA670038AA469911 AW006085 AI693790 AA872040 BE467580 BE467714 BE467700 AW971179AA431428 AA938692 AA416873 AA493619 AI671596 AW590794 AW016444 AI971108BE077433 C02533 AA593753 332567 8509_1 AW939251 NM_005252 AU076596V01512 V01512 AW579056 AA249247 AI590359 AW510478 AW518282 BE046054AW874080 AI268596 AA996237 AI695592 AI244117 AA290764 AA401957 AA505878AA428304 W74018 W74016 AA040944 AI272071 AA745909 AA620979 AA019816AI245094 AW009706 AA662536 AW024264 AI268601 AA932024 AW513222 AW024169AI659705 AA932526 AA975329 AI567603 AI889320 AA514238 AA020837 AI623966AA843677 AA477453 AA496353 AW372625 AV656426 K00650 W96348 N62388 R95977AA434270 AI093633 T27639 AW960245 AW881177 R15253 N36936 F07701 AA319315AA337290 AA284642 AA344052 F05184 AA351062 AA378451 AW794233 AW884380N36951 R49879 AB022276 AA300350 AW839435 AW191708 BE220350 AA280404AA485546 AW794235 AV654223 AW838891 AA295986 N72823 AA335648 AA371089AW845414 H63166 R12840 AA379680 AA477579 R13148 H71003 H71015 AA362156AW750674 AW845415 AA366924 AW608044 AI570388 R31511 R33906 R33921AW663022 AW360985 AI207838 AW607239 AI672451 AI573282 AW794752 AA370328AW998896 AW797239 AW998912 AW794742 AI954543 AI810067 AW073373 AA370325AW195330 C18106 AW998736 R79476 AA429721 AI891081 AI381534 AW022137AW020000 AI630329 N99428 AI870222 AI971257 AI922196 AI857753 AW579397D56749 AI925005 AI685727 AW805573 AI982678 AI784604 AI005625 AW877772AI634947 AI950829 AA493243 BE166086 AI801820 AI925643 AI627992 AW316704AI261318 D57757 AA887178 AW770406 AI972075 AI222254 AI675794 D58060AI701954 D58166 AI799500 AW805669 AW276098 AW874253 AI962991 AI248184AW996924 AI017462 AW022260 AI885957 BE176841 AA878863 AI697419 AW662094AI479529 BE177025 D57403 AA507952 AW664593 AW800998 AI985773 AA566089AA442759 AI624670 AI460284 AI800205 AI537788 AI537593 AI244382 AA583463AA922678 AA864382 AI610837 D58070 AA844283 AA947992 N73801 AI453821D58184 AI678887 AW243755 AA746085 D57742 AA757380 R44148 AA496403BE180303 AW363528 BE006616 D57395 AW805507 AW805511 AA617991 AI373585H30122 D57744 AW805501 D57691 D58148 AW873164 AW768483 D57601 AA777812AA837997 BE180123 D57599 AA485387 AW022208 D58096 N67917 W95944 AW805506D57518 D57990 AI074096 D56521 D58151 AA428720 D56648 D57778 AW805504D57750 D58108 AW021706 D57449 D57041 D58277 D56935 AI356974 D57023AA018712 H27631 D57851 D57514 D57268 D57468 AW805646 AI278945 D57323D56986 D57539 D57829 D58078 AW805515 AI348684 D57772 R74449 BE041558D56746 AW798485 D56640 AA985597 D56702 D56849 D56874 AW581419 AA470397D57591 AW798984 T27640 N66497 D56803 AA618186 AW805647 D57945 N23726D56637 N23730 D56992 BE176882 BE176839 BE176909 D56757 N68137 D56987AI559806 AA631437 D57464 D56718 C17030 T29278 D57377 AW021936 AW118330AA515358 D56610 AA494092 D56934 T97774 AI473546 R74350 R84834 AA579200D56616 C03207 D57391 N52416 D56928 R79209 D56925 AA020879 D45546AI858769 R20750 T09381 F01435 AW627906 D58202 AI933993 F01912 H27552AA174191 T16515 AW023216 AA434146 H83387 AI346751 V01512 V01512 AA576407AW365140 AA937471 BE174681 AI568829 AI274663 R85530 AL048225 H83388AW798734 332577 89088_2 AI826268 AW248872 H69511 AI748806 AW779557AI992254 AI890377 AW151271 AI356374 AI634503 AA777065 AI590131 H37767AI889058 H69512 AA046480 N27343 AI573008 AW130925 AI635838 AW594603AW000790 AI208239 AI275835 AW090294 AA021587 AW273456 AA505726 AW469424AI400222 AI025723 BE046148 AI128668 BE350462 AW302601 AI299977 AA284809AI640358 AW470364 AI241794 AA650048 AW090027 H15377 AW615318 D60021AI934336 AW118536 AI041281 AA614238 R85918 AW571741 AW516692 AW572232AW515188 AI798585 AI392825 Z40518 AI869580 AA469975 AI537819 AI810684AI701744 AI370410 BE383083 Z44676 BE002481 BE002532 AA456765 N44196D60022 C14604 AA021099 AA284872 BE266647 AW249292 332640 4172_1 BE568452BE297396 AA449593 AW732490 AW069736 BE548667 AA207229 AF044588 NM_003981BE268994 AW444578 AA471151 BE250747 AW732555 AA074582 BE336856 AW408764AA191159 BE092129 AA310614 AW958677 AA312276 AW750027 AW750046 AW750032AW750024 AA188893 AW750054 AW408409 AW750030 BE151875 AA478509 N58721AA195614 H70079 H75580 BE250401 AA454518 AA007263 AA626405 AA417152AA004230 AA557354 AW863151 AW863181 AA702179 AI924143 AI671185 BE006198AA190630 AI638795 AI609113 AI056239 BE537023 BE464668 AA634413 BE208066BE208833 AW250803 AI337375 AA478510 BE501624 AI814763 AW594726 AI091408AA827285 AA189108 AW594169 BE618589 BE618040 AL135398 AA632206 AI080026AI638180 AA725439 AI379107 AI288872 H14801 AI679151 AI263619 AI559213AI679722 W93249 AA552345 AA417030 AI969543 AA534494 AI038181 AA766364AA573241 AI754325 AW043937 BE207865 AI291838 N73585 N73539 AW805051AA808510 AI699813 AW166044 AW104716 H05808 AA248270 BE538022 N56013AA621586 AA149737 D19671 AW192890 N54283 H73339 AA910989 BE273424BE560082 AW959012 AA313552 AW750034 BE072537 BE297947 AW732361 AA449336D29574 332732 5436_1 AF191019 NM_015516 BE546494 AL110276 R13844BE313586 BE336912 R18704 R18703 AA045868 T70952 BE336901 T60387 BE149749BE271848 BE271902 AA489929 Z45402 T64360 AA305745 AA009451 T95706 H14907AA299901 C03221 T72431 AW471185 AA335297 AI269100 AA345072 AW965160H27581 R48910 H25380 AA335281 AW973283 T79590 AW183447 T64172 AI744097AI342358 AA336102 AA335299 BE208375 AI140834 AA088181 AI860314 AI738613T70902 R42077 AI884558 AA489798 AI130828 AA009735 H25381 AW612425 R48801H27507 H30105 H44671 AI631362 AA558470 AW014412 AA552059 AA045801AW589435 AI039657 H14614 AA974256 R42078 AI245758 T61886 AI559202AI074139 AI817313 AI041484 AA437138 AI613032 AI147891 AI457945 AW197727AI074399 AI758636 AI598048 AA972077 M85390 R36989 R71936 AI867492 T40081Z41115 AA772775 T41013 AI695691 T40996 AI826822 N93464 AW955524 AA088651Pkey: Unique Eos probeset identifier numberCAT number: Gene cluster numberAccession: Genbank accession numbers

TABLE 1C Pkey Ref Strand Nt_position 332792 Dunham, I. et.al. Plus73381-73768 333135 Dunham, I. et.al. Plus 3361208-3361369 333137 Dunham,I. et.al. Plus 3367643-3367726 333138 Dunham, I. et.al. Plus3369205-3369323 333139 Dunham, I. et.al. Plus 3369495-3369571 333516Dunham, I. et.al. Plus 5570204-5570390 333517 Dunham, I. et.al. Plus5570729-5570925 333795 Dunham, I. et.al. Plus 7807688-7807795 333796Dunham, I. et.al. Plus 7808253-7808319 333808 Dunham, I. et.al. Plus7880600-7880775 333809 Dunham, I. et.al. Plus 7880600-7880775 333845Dunham, I. et.al. Plus 8005832-8005945 333849 Dunham, I. et.al. Plus8018323-8018472 334101 Dunham, I. et.al. Plus 9973413-9973550 334616Dunham, I. et.al. Plus 15176123-15176470 334891 Dunham, I. et.al. Plus19299770-19299944 334899 Dunham, I. et.al. Plus 19315168-19315311 334900Dunham, I. et.al. Plus 19315678-19315743 334902 Dunham, I. et.al. Plus19317083-19317195 334905 Dunham, I. et.al. Plus 19322553-19322680 334906Dunham, I. et.al. Plus 19323493-19323590 335044 Dunham, I. et.al. Plus20842088-20842682 335149 Dunham, I. et.al. Plus 21497441-21497587 335809Dunham, I. et.al. Plus 26310772-26310909 335810 Dunham, I. et.al. Plus26314767-26314849 335824 Dunham, I. et.al. Plus 26376860-26376942 336054Dunham, I. et.al. Plus 29161685-29161937 336721 Dunham, I. et.al. Plus3371522-3371586 337182 Dunham, I. et.al. Plus 23934889-23934962 337674Dunham, I. et.al. Plus 3332616-3332697 337675 Dunham, I. et.al. Plus3335368-3335505 337755 Dunham, I. et.al. Plus 3971764-3971900 338038Dunham, I. et.al. Plus 8138219-8138392 338316 Dunham, I. et.al. Plus17089711-17089988 333124 Dunham, I. et.al. Minus 3318017-3317932 333743Dunham, I. et.al. Minus 7573218-7573060 334221 Dunham, I. et.al. Minus12730944-12730387 334222 Dunham, I. et.al. Minus 12732417-12732289334282 Dunham, I. et.al. Minus 13285293-13285178 334502 Dunham, I.et.al. Minus 14488605-14488526 334578 Dunham, I. et.al. Minus15004462-15004304 334951 Dunham, I. et.al. Minus 20147708-20147502335289 Dunham, I. et.al. Minus 22305950-22305708 335290 Dunham, I.et.al. Minus 22309950-22309891 335293 Dunham, I. et.al. Minus22316408-22316275 335682 Dunham, I. et.al. Minus 25421215-25421093335753 Dunham, I. et.al. Minus 25761535-25761444 335755 Dunham, I.et.al. Minus 25763806-25763747 335756 Dunham, I. et.al. Minus25764330-25764251 336662 Dunham, I. et.al. Minus 2158060-2157993 336684Dunham, I. et.al. Minus 2158060-2157993 337603 Dunham, I. et.al. Minus1299296-1299194 338561 Dunham, I. et.al. Minus 22311966-22311856 338562Dunham, I. et.al. Minus 22312594-22312465 339186 Dunham, I. et.al. Minus32339211-32339097 325889 5867087 Plus 223829-223891 330032 6682596 Plus85177-85237 330033 6682596 Plus 86663-86723 326213 5867224 Minus60751-60927 326816 6552458 Plus 198354-198436 327110 6117842 Plus94608-94785 327821 5867968 Plus 131060-131232 328164 5868068 Minus27080-27226 328648 6004473 Plus 424829-424959 329365 5868838 Minus107687-107765Pkey: Unique number corresponding to an Eos probesetRef: Sequence source. The 7 digit numbers in this column are GenbankIdentifier (GI) numbers. “Dunham I. et al.” refers to the publicationentitled “The DNA sequence of human chromosome 22.” Dunham I. et al.(1999) Nature 402: 489-495.Strand: Indicates DNA strand from which exons were predicted.Nt_position: Indicates nucleotide positions of predicted exons.Table 2A lists about 1165 genes selected to have an interestingexpression pattern during androgen withdrawal of prostate cancer tissue.These genes were selected by analysis of variance, such that the P valueis less than 0.01, the 90th percentile exhibits a minimum of 100 averageintensity across all samples, and a comparison of any group means showsa minimum 3 fold change. The interesting expression patterns can bebroadly defined into the following categories:1. Genes that are expressed early in the time course of androgenwithdrawal, then drop off in expression, and then express again withemergence of androgen-independence (hi-lo-lo-hi pattern in table 2A).2. Genes that are expressed early in the time course, then drop off inexpression immediately after androgen-withdrawal, and do sot expressagain with emergence of androgen-independence (hi-lo-lo-lo pattern intable 2A).3. Genes that are expressed early in the time course, then drop off inexpression after several days of androgen withdrawal, and do not expressagain with emergence of androgen-independence (hi-hi-lo-lo pattern intable 2A).4. Genes that are not expressed early in the time course, but expressonly with emergence of androgen-independence (lo-lo-lo-hi pattern intable 2A).5. Genes that are not expressed early in the time course, but thenexpress as androgen is withdrawn and continue to express with emergenceof androgen-independence (lo-lo-hi-hi pattern in table 2A).6. Genes that are not expressed early in the time course, but thenexpress as androgen is withdrawn and drop off again with emergence ofandrogen-independence (lo-lo-hi-lo pattern in table 2A).Table 2B lists accession numbers for primekeys lacking a unigeneID intable 2A. For each probeset is listed a gene cluster number from whicholigonucleotides were designed. Gene clusters were compiled usingsequences derived from Genbank ESTs and mRNAs. These sequences wereclustered based on sequence similarity using Clustering and AlignmentTools (Double Twist, Oakland Calif.). Genbank accession numbers forsequences comprising each cluster are listed in the “Accession” column.

Table 2C lists genomic positioning for primekeys lacking unigene ID'sand accession numbers in table 2A. For each predicted exon is listedgenomic sequence source used for prediction. Nucleotide locations ofeach predicted exon are also listed TABLE 2A ABOUT 1165 GENES SELECTEDTO HAVE AN INTERESTING EXPRESSION PATTERN DURING ANDROGEN WITHDRAWAL OFPROSTATE CANCER TISSUE Pkey ExAccn UnigeneID Unigene Title Pattern433412 AV653729 Hs.8185 CGI-44 protein; sulfide dehydrogenase lilo—lo-hi-lo 429097 AK001270 Hs.196086 hypothetical protein FLJ10408lo—lo-hi-lo 442731 AI868167 Hs.131044 ESTs lo—lo-hi-lo 420820 W26096Hs.336635 Homo sapiens, clone IMAGE: 4179482, mRNA lo—lo-hi-lo 422267AB033044 Hs.114012 KIAA1218 protein lo—lo-hi-lo 416953 N31537 Hs.269046ESTs lo—lo-hi-lo 413277 H24177 Hs.75262 cathepsin O lo—lo-hi-lo 410209AI583661 Hs.60548 hypothetical protein PRO1635 lo—lo-hi-lo 428523AW974540 Hs.98626 ESTs lo—lo-hi-lo 435847 W93821 Hs.39780 CDA017 proteinlo—lo-hi-lo 443967 AW294013 Hs.200942 ESTs lo—lo-hi-lo 440838 AA907075Hs.131307 ESTs lo—lo-hi-lo 404054 Target Exon lo—lo-hi-lo 431697 H66740Hs.38540 ESTs, Weakly similar to ALU4_HUMAN ALU S lo—lo-hi-lo 432114AL036021 Hs.8934 ESTs lo—lo-hi-lo 446397 AW275603 Hs.200712 ESTslo—lo-hi-lo 414094 H15088 Hs.31433 ESTs lo—lo-hi-lo 424005 AB033041Hs.137507 vang (van gogh, Drosophila)-like 2 lo—lo-hi-lo 424401 H67220Hs.169681 death effector domain-containing lo—lo-hi-lo 449749 AI668611Hs.49760 ESTs lo—lo-hi-lo 458368 BE504731 Hs.138827 ESTs lo—lo-hi-lo427221 L15409 Hs.174007 von Hippel-Lindau syndrome lo—lo-hi-lo 432715AA247152 Hs.200483 ESTs, Weakly similar to KIAA1074 protein lo—lo-hi-lo425980 AA366951 gb: EST77963 Pancreas tumor III Homo sapi lo—lo-hi-lo412492 AW962604 gb: EST374677 MAGE resequences, MAGG Homo lo—lo-hi-lo438882 AA827695 gb: od56c02.s1 NCI_CGAP_GCB1 Homo sapiens lo—lo-hi-lo422473 U94780 Hs.117242 meningioma expressed antigen 6 (coiled-clo—lo-hi-lo 404211 NM_005936: Homo sapiens myeloid/lymphoid lo—lo-hi-lo423019 AI640185 Hs.283626 ESTs lo—lo-hi-lo 443559 AI076765 Hs.269899ESTs, Moderately similar to ALU8_HUMAN A lo—lo-hi-lo 444291 AI598022Hs.193989 TAR DNA binding protein lo—lo-hi-lo 428065 AI634046 Hs.157313ESTs lo—lo-hi-lo 442566 R37337 Hs.12111 ESTs lo—lo-hi-lo 442202 BE272862Hs.106534 hypothetical protein FLJ22625 lo—lo-hi-lo 439456 AI752409Hs.109314 hypothetical protein FLJ20980 lo—lo-hi-lo 423476 AL035633Human DNA sequence from clone RP5-1046G1 lo—lo-hi-lo 437952 D63209Hs.5944 solute carrier family 11 (proton-coupled lo—lo-hi-lo 451987AA815092 Hs.77554 Homo sapiens cDNA FLJ14967 fis, clone TH lo—lo-hi-lo453408 AI804732 Hs.295963 ESTs lo—lo-hi-lo 444004 N39842 Hs.301444KIAA1673 lo—lo-hi-lo 452691 AA164842 Hs.192619 KIAA1600 proteinlo—lo-hi-lo 434865 AW050449 Hs.116507 ESTs lo—lo-hi-lo 440819 AI809444Hs.202108 ESTs lo—lo-hi-lo 419526 AI821895 Hs.193481 ESTs lo—lo-hi-lo422072 AB018255 Hs.111138 KIAA0712 gene product lo—lo-hi-lo 453459BE047032 Hs.257789 ESTs lo—lo-hi-lo 419038 AW134924 Hs.190325 ESTslo—lo-hi-lo 413243 AA769266 Hs.193657 ESTs lo—lo-hi-lo 432079 AW972746gb: EST384840 MAGE resequences, MAGL Homo lo—lo-hi-lo 441328 AI982794Hs.159473 ESTs lo—lo-hi-lo 416508 R39769 ESTs, Moderately similar toALU8_HUMAN A lo—lo-hi-lo 451066 AI758660 Hs.206132 ESTs lo—lo-hi-lo446017 N98238 Hs.55185 ESTs lo—lo-hi-lo 447104 R19085 Hs.210706 Homosapiens cDNA FLJ13182 fis, clone NT lo—lo-hi-lo 447211 AL161961 Hs.17767KIAA1554 protein lo—lo-hi-lo 447765 AW014112 Hs.161390 ESTs lo—lo-hi-lo429540 M85776 gb: EST02297 Fetal brain, Stratagene (cat lo—lo-hi-lo444314 AI140497 gb: ow76b09.s1 Soares_fetal_liver_spleen_(—) lo—lo-hi-lo414555 N98569 Hs.76422 phospholipase A2, group IIA (platelets,lo—lo-hi-lo 432677 NM_004482 Hs.278611UDP-N-acetyl-alpha-D-galactosamine: polyp lo—lo-hi-lo 422091 AI906339Hs.97927 ESTs lo—lo-hi-lo 423028 H90946 gb: yu86c02.r1 Soares fetalliver spleen lo—lo-hi-lo 444040 AF204231 Hs.182982 golgin-67 lo—lo-hi-lo441111 AI806867 Hs.126594 ESTs lo—lo-hi-lo 418838 AW385224 Hs.35198ectonucleotide pyrophosphatase/phosphodi lo—lo-hi-lo 415999 AA172179Hs.294029 ESTs lo—lo-hi-lo 429615 AF258627 Hs.211562 ATP-bindingcassette, sub-family A (ABC1 lo—lo-hi-lo 427774 AA278583 Hs.180737 Homosapiens clone 23664 and 23905 mRNA lo—lo-hi-lo 438585 AA811371 Hs.123362ESTs lo—lo-hi-lo 424776 AI867931 Hs.164595 ESTs lo—lo-hi-lo 413786AW613780 Hs.13500 ESTs lo—lo-hi-lo 421077 AK000061 Hs.101590hypothetical protein lo—lo-hi-lo 445837 AI261700 Hs.145544 ESTslo—lo-hi-lo 449282 AL048056 Hs.23437 Homo sapiens cDNA FLJ13555 fis,clone PL lo—lo-hi-lo 414065 AW515373 Hs.271249 Homo sapiens cDNAFLJ13580 fis, clone PL lo—lo-hi-lo 432527 AW975028 Hs.102754 ESTslo—lo-hi-lo 412093 BE242691 Hs.14947 ESTs lo—lo-hi-lo 457121 AI743770Hs.180513 ESTs, Weakly similar to KIAA0822 protein lo—lo-hi-lo 417280AW173116 Hs.250103 ESTs lo—lo-hi-lo 452445 AB002438 Hs.29596 Homosapiens mRNA from chromosome 5q21-2 lo—lo-hi-lo 438624 AA889055Hs.123468 ESTs lo—lo-hi-lo 442343 AA992480 Hs.129874 ESTs lo—lo-hi-lo401416 C14000338*: gi|7459502|pir||S74665 outer lo—lo-hi-lo 437176AW176909 Hs.42346 calcineurin-binding protein calsarcin-1 lo—lo-hi-lo451663 AI872360 Hs.209293 ESTs lo—lo-hi-lo 449295 AW137268 Hs.270954ESTs lo—lo-hi-lo 426848 H72531 Hs.36190 ESTs lo—lo-hi-lo 445467 AI239832Hs.15617 ESTs, Weakly similar to ALU4_HUMAN ALU S lo—lo-hi-lo 418662AI801098 Hs.151500 ESTs lo—lo-hi-lo 416239 AL038450 Hs.48948 ESTslo—lo-hi-lo 428054 AI948688 Hs.266619 ESTs lo—lo-hi-lo 435284 AA879470Hs.96849 Homo sapiens cDNA FLJ11492 fis, clone HE lo—lo-hi-lo 424332AA338919 Hs.101615 ESTs lo—lo-hi-lo 442369 AI565071 Hs.159983 ESTslo—lo-hi-lo 420717 AA284447 Hs.271887 ESTs lo—lo-hi-lo 439584 AA838114Hs.221612 ESTs lo—lo-hi-lo 440260 AI972867 Hs.7130 copine IV lo—lo-hi-lo426269 H15302 Hs.168950 Homo sapiens mRNA; cDNA DKFZp566A1046 (flo—lo-hi-lo 428398 AI249368 Hs.98558 ESTs lo—lo-hi-lo 407276 AI951118Hs.326736 Homo sapiens breast cancer antigen NY-BR lo—lo-hi-lo 409339AB020686 Hs.54037 ectonucleotide pyrophosphatase/phosphodi lo—lo-hi-lo442150 AJ368158 Hs.70983 PTPL1-associated RhoGAP 1 lo—lo-hi-lo 415787H01463 Hs.93534 ESTs lo—lo-hi-lo 430685 AI690234 Hs.191666 ESTs, Weaklysimilar to GNMSLL retroviru lo—lo-hi-lo 443794 N94104 Hs.29280 ESTslo—lo-hi-lo 446215 AW821329 Hs.14368 SH3 domain binding glutamicacid-rich pr lo—lo-hi-lo 441285 NM_002374 Hs.167 microtubule-associatedprotein 2 lo—lo-hi-lo 448738 BE614081 gb: 601503815F1 NIH_MGC_71 Homosapiens c lo—lo-hi-lo 403746 ENSP00000226812*: KIAA1494 protein (Fragmlo—lo-hi-lo 434022 R18374 Hs.117956 ESTs lo—lo-hi-lo 435714 AA699325Hs.269880 ESTs lo—lo-hi-lo 439848 AW979249 gb: EST391359 MAGEresequences, MAGP Homo lo—lo-hi-lo 421974 AA301270 gb: EST14192 Testistumor Homo sapiens cD lo—lo-hi-lo 433332 AI367347 Hs.44898 Homo sapiensclone TCCCTA00151 mRNA sequ lo—lo-hi-lo 449919 AI674685 Hs.200141 ESTslo—lo-hi-lo 407192 AA609200 gb: af12e02.s1 Soares_testis_NHT Homo saplo—lo-hi-lo 436169 AA888311 Hs.17602 Homo sapiens cDNA FLJ12381 fis,clone MA lo—lo-hi-lo 418624 AI734080 Hs.104211 ESTs lo—lo-hi-lo 432432AA541323 Hs.115831 ESTs lo—lo-hi-lo 426172 AA371307 Hs.125056 ESTslo—lo-hi-lo 401093 C12000586*: gi|6330167|dbj|BAA86477.1| (A lo—lo-hi-lo426716 NM_006379 Hs.171921 sema domain, immunoglobulin domain (Ig),lo—lo-hi-lo 439569 AW602166 Hs.222399 CEGP1 protein lo—lo-hi-lo 451720AW970985 Hs.290853 ESTs lo—lo-hi-lo 429163 AA884766 gb: am20a10.s1Soares_NFL_T_GBC_S1 Homo s lo—lo-hi-lo 432435 BE218886 Hs.282070 ESTslo—lo-hi-lo 408170 AW204516 Hs.31835 ESTs lo—lo-hi-lo 433530 BE349534Hs.281789 ESTs lo—lo-hi-lo 425776 U25128 Hs.159499 parathyroid hormonereceptor 2 lo—lo-hi-lo 430068 AA464964 gb: zx80f10.s1 Soares ovary tumorNbHOT H lo—lo-hi-lo 422725 AA315703 Hs.199993 ESTs, Weakly similar toALUB_HUMAN !!!! lo—lo-hi-lo 432314 AA533447 Hs.312989 ESTs lo—lo-hi-lo434609 R76593 gb: yi60c11.r1 Soares placenta Nb2HP Homo lo—lo-hi-lo448760 AA313825 Hs.21941 AD036 protein lo—lo-hi-lo 417381 AF164142Hs.82042 solute carrier family 23 (nucleobase tra lo—lo-hi-lo 456334T50392 Hs.271745 ESTs lo—lo-hi-lo 435445 AA737345 Hs.294041 ESTslo—lo-hi-lo 411928 AA888624 Hs.197289 rab3 GTPase-activating protein,non-cata lo—lo-hi-lo 438869 AF075009 gb: Homo sapiens full length insertcDNA lo—lo-hi-lo 423932 T95633 Hs.189703 ESTs lo—lo-hi-lo 422222AI699372 Hs.193247 hypothetical protein DKFZp434A171 lo—lo-hi-lo 434941AW073202 Hs.334825 Homo sapiens cDNA FLJ14752 fis, clone NT lo—lo-hi-lo415736 AA827082 Hs.291872 ESTs lo—lo-hi-lo 432722 AA830532 Hs.326150ESTs lo—lo-hi-lo 435511 AA683336 Hs.189046 ESTs lo—lo-hi-lo 432242AW022715 Hs.162160 ESTs, Weakly similar to ALU4_HUMAN ALU S lo—lo-hi-lo451141 AW772713 Hs.247186 ESTs lo—lo-hi-lo 450546 AA010200 Hs.175551ESTs lo—lo-hi-lo 413351 BE086815 ESTs lo—lo-hi-lo 439324 AF086134Hs.94309 ESTs lo—lo-hi-lo 452688 AA721140 Hs.49930 ESTs, Weakly similarto putative p150 [H lo—lo-hi-lo 415669 NM_005025 Hs.78589 serine (orcysteine) proteinase inhibito lo—lo-hi-lo 450164 AI239923 Hs.63931 ESTslo—lo-hi-lo 417169 R13550 Hs.246773 ESTs lo—lo-hi-lo 443645 R36475Hs.24321 Homo sapiens cDNA FLJ12028 fis, clone HE lo—lo-hi-lo 424878H57111 Hs.221132 ESTs lo—lo-hi-lo 449618 AI076459 Hs.15978 KIAA1272protein lo—lo-hi-lo 432572 AI660840 Hs.191202 ESTs, Weakly similar toALUE_HUMAN !!!! lo—lo-hi-lo 400293 N51002 Hs.306480 Homo sapiens mRNA;cDNA DKFZp761E2112 (f lo—lo-hi-lo 431474 AL133990 Hs.190642 CEGP1protein lo—lo-hi-lo 421674 T10707 Hs.296355 hypothetical proteinFLJ23138 lo—lo-hi-lo 438494 AA908678 Hs.130183 ESTs lo—lo-hi-lo 425332AA633306 Hs.127279 ESTs lo—lo-hi-lo 451411 AA017492 Hs.135655 ESTlo—lo-hi-lo 419972 AL041465 Hs.182982 golgin-67 lo—lo-hi-lo 434804AA649530 Hs.348148 gb: ns44f05.s1 NCI_CGAP_Alv1 Homo sapiens lo—lo-hi-lo442832 AW206560 Hs.253569 ESTs lo—lo-hi-lo 408660 AA525775 ESTs,Moderately similar to PC4259 ferri lo—lo-hi-lo 432674 AA641092 Hs.257339ESTs, Weakly similar to I38022 hypotheti lo—lo-hi-lo 448150 AI472167ESTs lo—lo-hi-lo 450468 AW379075 Hs.141742 Homo sapiens cDNA FLJ12211fis, clone MA lo—lo-hi-lo 452874 AK001061 Hs.30925 hypothetical proteinFLJ10199 lo—lo-hi-lo 412088 AI689496 Hs.108932 ESTs lo—lo-hi-lo 443451AI057404 Hs.58698 ESTs lo—lo-hi-lo 453853 AL040600 Hs.188083 ESTslo—lo-hi-lo 419863 AW952691 Hs.93485 Homo sapiens mRNA; cDNADKFZp761D191 (fr lo—lo-hi-lo 420729 AW964897 Hs.290825 ESTs lo—lo-hi-lo440801 AA906366 Hs.190535 ESTs lo—lo-hi-lo 407284 AI539227 Hs.214039hypothetical protein FLJ23556 lo—lo-hi-lo 428279 AA425310 Hs.155766ESTs, Weakly similar to A47582 B-cell gr lo—lo-hi-lo 436862 AI821940ESTs, Moderately similar to ALU8_HUMAN A lo—lo-hi-lo 432340 AA534222 gb:nj21d02.s1 NCI_CGAP_AA1 Homo sapiens lo—lo-hi-lo 442048 AA974603 gb:op34f05.s1 Soares_NFL_T_GBC_S1 Homo s lo—lo-hi-lo 418781 T41160 Hs.8404ESTs lo—lo-hi-lo 450642 R39773 Hs.7130 copine IV lo—lo-hi-lo 451661AB020650 Hs.26777 Homo sapiens, Similar to KIAA0843 protei lo—lo-hi-lo435812 AA700439 Hs.188490 ESTs lo—lo-hi-lo 448065 AI459177 Hs.172759ESTs, Moderately similar to ALU7_HUMAN A lo—lo-hi-lo 453486 AL039201Hs.173554 ubiquinol-cytochrome c reductase core pr lo—lo-hi-lo 414312AA155694 Hs.191060 ESTs lo—lo-hi-lo 438980 AW502384 gb:UI-HF-BR0p-aka-f-12-0-UI.r1 NIH_MGC_5 lo—lo-hi-lo 408001 AA046458Hs.95296 ESTs lo—lo-hi-lo 421476 AW953805 Hs.21887 ESTs lo—lo-hi-lo414426 D60745 Hs.25925 Homo sapiens, clone MGC: 15393, mRNA, comlo—lo-hi-lo 444563 N57057 Hs.284163 ANKHZN protein lo—lo-hi-lo 418771AA807881 Hs.25329 ESTs lo—lo-hi-lo 417843 W07361 Hs.22545 Homo sapienscDNA FLJ12935 fis, clone NT lo—lo-hi-lo 415565 AA642449 Hs.48994 ESTs,Weakly similar to AF151800 1 CGI-4 lo—lo-hi-lo 419229 AI827237 Hs.282884ESTs lo—lo-hi-lo 419905 AW248229 Hs.93659 protein disulfide isomeraserelated prot lo—lo-hi-lo 452870 AW502761 Hs.30909 KIAA0430 gene productlo—lo-hi-lo 449059 AK000566 Hs.98135 hypothetical protein FLJ20559lo—lo-hi-lo 416157 NM_003243 Hs.342874 transforming growth factor, betarecepto lo—lo-hi-lo 439305 AW393883 Hs.98968 hypothetical proteinFLJ23058 lo—lo-hi-lo 419235 AW470411 Hs.288433 neurotrimin lo—lo-hi-lo416640 BE262478 Hs.79404 neuron-specific protein lo—lo-hi-lo 434938AW500718 Hs.8115 Homo sapiens, clone MGC: 16169, mRNA, com lo—lo-hi-lo408177 AI241733 Hs.43871 ESTs lo—lo-hi-lo 438459 T49300 Hs.35304 Homosapiens cDNA FLJ13655 fis, clone PL lo—lo-hi-lo 418381 AA682393Hs.119237 ESTs lo—lo-hi-lo 432161 AK000400 Hs.341181 ESTs, Weaklysimilar to envelope [H. sapi lo—lo-hi-lo 418283 S79895 Hs.83942cathepsin K (pycnodysostosis) lo—lo-hi-lo 421443 BE550141 Hs.156148hypothetical protein FLJ13231 lo—lo-hi-lo 416619 AF013168 Hs.79393tuberous sclerosis 1 lo—lo-hi-lo 449802 AW901804 Hs.23984 hypotheticalprotein FLJ20147 lo—lo-hi-lo 446714 W73818 Hs.110028 ESTs lo—lo-hi-lo413195 AA127382 Hs.22404 protease, serine, 12 (neurotrypsin, motolo—lo-hi-lo 438233 W52448 Hs.56147 ESTs lo—lo-hi-lo 416051 AA835868Hs.25253 mannosidase, alpha, class 1A, member 1 lo—lo-hi-lo 438855AW946276 Hs.6441 Homo sapiens mRNA; cDNA DKFZp586J021 (fr lo—lo-hi-lo425907 AA365752 Hs.155965 ESTs lo—lo-hi-lo 451295 AI557212 Hs.17132ESTs, Moderately similar to I54374 gene lo—lo-hi-lo 415443 T07353Hs.7948 ESTs lo—lo-hi-lo 422366 T83882 Hs.97927 ESTs lo—lo-hi-lo 435163AA668884 Hs.19155 ESTs lo—lo-hi-lo 426559 AB001914 Hs.170414 pairedbasic amino acid cleaving system lo—lo-hi-lo 448988 Y09763 Hs.22785gamma-aminobutyric acid (GABA) A recepto lo—lo-hi-lo 453655 AW960427Hs.342874 transforming growth factor, beta recepto lo—lo-hi-lo 414516AI307802 Hs.135560 ESTs, Weakly similar to T43458 hypotheti lo—lo-hi-lo420028 AB014680 Hs.8786 carbohydrate (N-acetylglucosamine-6-O) slo—lo-hi-lo 430223 NM_002514 Hs.235935 nephroblastoma overexpressed genelo—lo-hi-lo 425887 AL049443 Hs.161283 Homo sapiens mRNA; cDNADKFZp586N2020 (f lo—lo-hi-lo 442577 AA292998 Hs.163900 ESTs lo—lo-hi-lo424940 AA985308 Hs.283902 ESTs lo—lo-hi-lo 428839 AI767756 Hs.82302 Homosapiens cDNA FLJ14814 fis, clone NT lo—lo-hi-lo 443868 W88483 Hs.293650Homo sapiens mRNA for RGPR-p117, complet lo—lo-hi-lo 430334 AI824719Hs.328700 ESTs lo—lo-hi-lo 439686 W40445 Hs.235857 ESTs, Weakly similarto I38022 hypotheti lo—lo-hi-lo 423754 NM_016181 Hs.132526 melanomaantigen lo—lo-hi-lo 415205 H71616 Hs.135233 ESTs lo—lo-hi-lo 426413AA377823 gb: EST90805 Synovial sarcoma Homo sapien lo—lo-hi-lo 407204R41933 Hs.140237 ESTs, Weakly similar to ALU1_HUMAN ALU S lo—lo-hi-lo430234 N29317 Hs.236463 KIAA1238 protein lo—lo-hi-lo 437143 AW204056Hs.8917 ESTs lo—lo-hi—hi 445162 AB011131 Hs.12376 piccolo (presynapticcytomatrix protein) lo—lo-hi—hi 415083 AI632683 Hs.27179 Homo sapienscDNA FLJ12933 fis, clone NT lo—lo-hi—hi 442924 AA533513 Hs.93659 proteindisulfide isomerase related prot lo—lo-hi—hi 429536 AA873016 Hs.206097oncogene TC21 lo—lo-hi—hi 458584 AF217518 Hs.324136 PTD012 proteinlo—lo-hi—hi 419647 AA348947 Hs.91816 hypothetical protein lo—lo-hi—hi427201 AB037860 Hs.173933 nuclear factor I/A lo—lo-hi—hi 428030 AI915228Hs.11493 Homo sapiens cDNA FLJ13536 fis, clone PL lo—lo-hi—hi 411779AA292811 Hs.72050 non-metastatic cells 5, protein expresse lo—lo-hi—hi442482 NM_014039 Hs.8360 PTD012 protein lo—lo-hi—hi 417458 NM_005655Hs.82173 TGFB inducible early growth response lo—lo-hi—hi 438021AV653790 Hs.324275 WW domain-containing protein 1 lo—lo-hi—hi 409799D11928 Hs.76845 phosphoserine phosphatase-like lo—lo-hi—hi 440676NM_004987 Hs.112378 LIM and senescent cell antigen-like doma lo—lo-hi—hi421437 AW821252 Hs.104336 hypothetical protein lo—lo-hi—hi 456362AW973003 Hs.179909 hypothetical protein FLJ22995 lo—lo-hi—hi 407686AW901268 Hs.126043 chromosome 21 open reading frame 51 lo—lo-hi—hi431129 AL137751 Hs.263671 Homo sapiens mRNA; cDNA DKFZp434I0812 (flo—lo-hi—hi 431874 AW610031 Hs.323914 translocase of inner mitochondrialmembr lo—lo-hi—hi 448072 AI459306 Hs.24908 ESTs lo—lo-hi—hi 436860H12751 Hs.5327 PRO1914 protein lo—lo-hi—hi 448770 AA326683 Hs.21992likely ortholog of mouse variant polyade lo—lo-hi—hi 428044 AA093322Hs.301404 RNA binding motif protein 3 lo—lo-hi—hi 451468 AW503398Hs.293663 ESTs, Moderately similar to I38022 hypot lo—lo-hi—hi 440278BE560870 Hs.9052 ESTs, Weakly similar to 2004399A chromos lo—lo-hi—hi441102 AA973905 intermediate filament protein Syncoilin lo—lo-hi—hi423942 AF209704 Hs.135723 glycolipid transfer protein lo—lo-hi—hi 425254U91985 Hs.105658 DNA fragmentation factor, 45 kD, alpha p lo—lo-hi—hi409324 W76202 Hs.343812 lipoic acid synthetase lo—lo-hi—hi 431707 R21326Hs.267905 hypothetical protein FLJ10422 lo—lo-hi—hi 423335 AB018337Hs.127287 KIAA0794 protein lo—lo-hi—hi 429200 AA447871 Hs.194215 ESTs,Weakly similar to I38022 hypotheti lo—lo-hi—hi 429898 AW117322 Hs.42366ESTs lo—lo-hi—hi 409604 AW444448 Hs.49124 ESTs lo—lo-hi—hi 431797BE169641 Hs.270134 hypothetical protein FLJ20280 lo—lo-hi—hi 437576BE514383 prothymosin, alpha (gene sequence 28) lo—lo-hi—hi 415992 C05837Hs.145807 hypothetical protein FLJ13593 lo—lo-hi—hi 458537 W24704Hs.54773 ESTs lo—lo-hi—hi 417665 AW852858 Hs.22862 ESTs lo—lo-hi—hi422292 AI815733 Hs.114360 transforming growth factor beta-stimulatlo—lo-hi—hi 421501 M29971 Hs.1384 O-6-methylguanine-DNAmethyltransferase lo—lo-hi—hi 457952 U25750 Human chromosome 17q21 mRNAclone 1046: 1 lo—lo-hi—hi 414630 BE410857 Hs.16064 gb: 601301177F1NIH_MGC_21 Homo sapiens c lo—lo-hi—hi 421990 T31811 Hs.110480 DC12protein lo—lo-hi—hi 404956 C1003210*: gi|6912582|ref|NP_036524.1| pelo—lo-hi—hi 436829 AW297958 Hs.163109 ESTs lo—lo-hi—hi 402106 AK002178hypothetical protein FLJ11316 lo—lo-hi—hi 404384 NM_020632*: Homosapiens ATPase, H(+)-tra lo—lo-hi—hi 445123 AI762911 Hs.145369 ESTslo—lo-hi—hi 401757 Target Exon lo—lo-hi—hi 439502 AA836672 Hs.130694ESTs lo—lo-hi—hi 400111 Eos Control lo—lo-hi—hi 405446 AI015709 Homosapiens mRNA; cDNA DKFZp586I2022 (f lo—lo-hi—hi 401563 C15001262:gi|7304981|ref|NP_038528.1| ca lo—lo-hi—hi 402786 C1000887*:gi|12732453|ref|XP_011474.1| C lo—lo-hi—hi 426484 AA379658 Hs.272759KIAA1457 protein lo—lo-hi—hi 414343 AL036166 Hs.323378 coated vesiclemembrane protein lo—lo-hi—hi 421970 AF227156 Hs.110103 RNApolymerase|transcription factor RR lo—lo-hi—hi 422592 BE081857 Hs.94211rcd1 (required for cell differentiation, lo—lo-hi—hi 413431 AW246428Hs.75355 ubiquitin-conjugating enzyme E2N (homolo lo—lo-hi—hi 426746J03626 Hs.2057 uridine monophosphate synthetase (orotat lo—lo-hi—hi400237 NM_001087*: Homo sapiens angio-associated lo—lo-hi—hi 402532Target Exon lo—lo-hi—hi 402396 Target Exon lo—lo-hi—hi 459649 AW298364Hs.289292 ESTs lo—lo-hi—hi 401512 NM_014080: Homo sapiens dualoxidase-like lo—lo-hi—hi 448622 AL046508 Hs.270607 ESTs, Weakly similarto STK2_HUMAN SERIN lo—lo-hi—hi 400501 ENSP00000251912*: KIAA1617protein (Fragm lo—lo-hi—hi 452324 W81486 Hs.58648 ESTs lo—lo-hi—hi453146 AI338952 Hs.32194 ESTs lo—lo-hi—hi 430445 AW892432 Hs.65307 ESTslo—lo-hi—hi 401750 NM_012448*: Homo sapiens signal transduce lo—lo-hi—hi435236 T03890 Hs.157208 ESTs, Highly similar to ARX MOUSE HOMEOBlo—lo-hi—hi 400375 NM_014115 NM_014115*: Homo sapiens PRO0113 proteinlo—lo-hi—hi 412151 AA100529 Hs.286232 Homo sapiens cDNA: FLJ23190 fis,clone L lo—lo-hi—hi 410498 AA355749 gb: EST64459 Jurkat T-cells VI Homosapie lo—lo-hi—hi 405044 NM_014630*: Homo sapiens KIAA0211 gene prlo—lo-hi—hi 413169 AW161061 Hs.62954 ESTs, Weakly similar to zinc fingerprot lo—lo-hi—hi 402101 ENSP00000217725*: Laminin alpha-1 chain plo—lo-hi—hi 455019 AW850818 gb: IL3-CT0220-091199-026-A03 CT0220 Homolo—lo-hi—hi 446826 AK000626 Hs.16230 hypothetical protein FLJ20619lo—lo-hi—hi 412180 AW898791 Hs.118837 gb: CM0-NN0075-130400-332-f06NN0075 Homo lo—lo-hi—hi 407273 AJ132560 gb: Homo sapiens mRNA forimmunoblobulin lo—lo-hi—hi 452895 BE389229 Hs.30954 phosphomevalonatekinase lo—lo-hi—hi 416117 H19480 Hs.268787 ESTs lo—lo-hi—hi 430934AI792302 Hs.248141 potassium inwardly-rectifying channel, s lo—lo-hi—hi416309 R84694 Hs.79194 cAMP responsive element binding proteinlo—lo-hi—hi 444578 T80795 Hs.193702 ESTs lo—lo-hi—hi 401966 C17000574:gi|8923190|ref|NP_060178.1| hy lo—lo-hi—hi 444850 AW444882 Hs.148483ESTs lo—lo-hi—hi 403885 Target Exon lo—lo-hi—hi 405435 Target Exonlo—lo-hi—hi 422694 C06003 Hs.23782 hypothetical protein FLJ12847lo—lo-hi—hi 422912 AW405973 Hs.11637 ESTs lo—lo-hi—hi 412748 BE083158Hs.10862 Homo sapiens cDNA: FLJ23313 fis, clone H lo—lo-hi—hi 403704Target Exon lo—lo-hi—hi 440507 H06994 gb: yl81b07.r1 Soares infant brain1NIB H lo—lo-hi—hi 405503 C7000609*: gi|628012|pir||A53933 myosin|lo—lo-hi—hi 456123 R00602 gb: ye74c04.r1 Soares fetal liver spleenlo—lo-hi—hi 454261 AF216077 Hs.48376 Homo sapiens clone HB-2 mRNAsequence lo—lo-hi—hi 458956 BE220675 gb: ht98f11.x1 NCI_CGAP_Lu24 Homosapiens lo—lo-hi—hi 418367 AA326035 Hs.59236 hypothetical proteinDKFZp434L0718 lo—lo-hi—hi 444553 AI167530 Hs.149380 ESTs lo—lo-hi—hi405811 NM_024810: Homo sapiens hypothetical prot lo—lo-hi—hi 429461AI188219 Hs.99311 ESTs, Weakly similar to HSJ2_HUMAN DNAJ lo—lo-hi—hi423378 BE313601 Hs.164866 hypothetical protein FLJ22558 lo—lo-hi—hi458516 BE010749 Hs.255097 ESTs lo—lo-hi—hi 404039 ENSP00000247650*:Hypothetical 177.6 kDa lo—lo-hi—hi 454148 AW732837 Hs.42390nasopharyngeal carcinoma susceptibility lo—lo-hi—hi 412678 AA115575Hs.114914 ESTs lo—lo-hi—hi 449298 AI911333 Hs.171689 ESTs lo—lo-hi—hi405525 NM_002439*: Homo sapiens mutS (E. coli) h lo—lo-hi—hi 424576BE154142 Hs.96833 ESTs lo—lo-hi—hi 451601 N92100 Hs.97437 centrosomalprotein 1 lo—lo-hi—hi 422395 AA310177 Hs.103931 DKFZP434B0335 proteinlo—lo-hi—hi 434333 AA186733 Hs.292154 stromal cell protein lo—lo-hi—hi413509 BE145419 gb: IL5-HT0198-291099-009-E01 HT0198 Homo lo—lo-hi—hi419504 AI088585 Hs.118904 ESTs lo—lo-hi—hi 448586 AF285120 Hs.283734CGI-204 protein lo—lo-hi—hi 401209 C12000519:gi|7710046|ref|NP_057914.1| ki lo—lo-hi—hi 423554 M90516 Hs.1674glutamine-fructose-6-phosphate transamin lo—lo-hi—hi 439803 AA001021Hs.6685 thyroid hormone receptor interactor 8 lo—lo-hi—hi 424593AA343729 gb: EST49730 Gall bladder|Homo sapiens lo—lo-hi—hi 408122AI432652 Hs.42824 hypothetical protein FLJ10718 lo—lo-hi—hi 409958NM_001523 Hs.57697 hyaluronan synthase 1 lo—lo-hi—hi 408214 AL120445Hs.77823 hypothetical protein FLJ21343 lo—lo-hi—hi 421911 AL041520 gb:DKFZp434G2317_s1 434 (synonym: htes3) lo—lo-hi—hi 407813 AL120247Hs.40109 KIAA0872 protein lo—lo-hi—hi 425211 M18667 Hs.1867progastricsin (pepsinogen C) lo—lo-hi—hi 442772 AW503680 Hs.5957 Homosapiens clone 24416 mRNA sequence lo—lo-hi—hi 419733 AW362955 Hs.224961Homo sapiens cDNA FLJ14415 fis, clone HE lo—lo-hi—hi 428260 AW290886Hs.86999 ESTs, Weakly similar to S65657 alpha-1C- lo—lo-hi—hi 427083NM_006363 Hs.173497 Sec23 (S. cerevisiae) homolog B lo—lo-hi—hi 418583AA604379 Hs.86211 hypothetical protein lo—lo-hi—hi 407355 AA846203Hs.193974 ESTs, Weakly similar to ALU1_HUMAN ALU S lo—lo-hi—hi 454003AA058944 Hs.116602 Homo sapiens, clone IMAGE: 4154008, mRNA, lo—lo-hi—hi425322 U63630 Hs.155637 protein kinase, DNA-activated, catalyticlo—lo-hi—hi 402240 Target Exon lo—lo-hi—hi 421867 AA481078 Hs.109045hypothetical protein FLJ10498 lo—lo-hi—hi 408603 R25283 Hs.326416 Homosapiens mRNA; cDNA DKFZp564H1916 (f lo—lo-hi—hi 437389 AL359587Hs.271586 hypothetical protein DKFZp762M115 lo—lo-hi—hi 457148 AF091035Hs.184627 KIAA0118 protein lo—lo-hi—hi 400277 Eos Control lo—lo-hi—hi400995 C11000295*: gi|12737279|ref|XP_012163.1| lo—lo-hi—hi 400818Target Exon lo—lo-hi—hi 402758 C1001899*: gi|12722636|ref|XP_010672.1| elo—lo-hi—hi 403708 Target Exon lo—lo-hi—hi 405610 ENSP00000241065*: CDNAlo—lo-hi—hi 414242 AA749230 Hs.26433 dolichyl-phosphate(UDP-N-acetylglucosam lo—lo-hi—hi 420757 X78592 Hs.99915 androgenreceptor (dihydrotestosterone r lo—lo-hi—hi 400965 C11002190*:gi|12737279|ref|XP_012163.1| lo—lo-hi—hi 401192 Target Exon lo—lo-hi—hi404407 Target Exon lo—lo-hi—hi 401405 Target Exon lo—lo-hi—hi 403055C2002219*: gi|12737280|ref|XP_006682.2| k lo—lo-hi—hi 404661 C9000306*:gi|12137280|ref|XP_006682.2| k lo—lo-hi—hi 433627 AF078666 Hs.284296Homo sapiens cDNA: FLJ22993 fis, clone K lo—lo-hi—hi 410204 AJ243425Hs.326035 early growth response 1 lo—lo-hi—hi 432642 BE297635 Hs.3069heat shock 70 kD protein 98 (mortalin-2) lo—lo-hi—hi 400769 Target Exonlo—lo-hi—hi 433980 AA137152 Hs.286049 phosphoserine aminotransferaselo—lo-hi—hi 403725 Target Exon lo—lo-hi—hi 413587 AA156164 Hs.286241protein kinase, cAMP-dependent, regulato lo—lo-hi—hi 422614 AI908006Hs.295362 Homo sapiens cDNA FLJ14459 fis, clone HE lo—lo-hi—hi 400275NM_006513*: Homo sapiens seryl-tRNA synth lo—lo-hi—hi 402810 NM_004930*:Homo sapiens capping protein lo—lo-hi—hi 452049 BE268289 Hs.27693peptidylprolyl isomerase (cyclophilin)-I lo—lo-hi—hi 445677 H96577Hs.6838 ras homolog gene family, member E lo—lo-hi—hi 428770 AK001667Hs.193128 hypothetical protein FLJ10805 lo—lo-hi—hi 428403 AI393048Hs.326159 leucine rich, repeat (in FLJI) interactin lo—lo-hi—hi 434647W74158 Hs.103189 lipopolysaccharide specific response-68 lo—lo-hi—hi402807 ENSP00000235229: SEMB. lo—lo-hi—hi 413992 W26276 Hs.136075 RNA,U2 small nuclear lo—lo-hi—hi 407191 AA608751 gb: ae56h07.s1 Stratagenelung carcinoma lo—lo-hi-lo 403328 Target Exon lo—lo-hi—hi 411984NM_005419 Hs.72988 signal transducer and activator of trans lo—lo-hi-lo451017 BE391847 Hs.181173 hypothetical protein MGC10771 lo—lo-hi—hi404108 C7000911*: gi|4235142|gb|AAD14470.1| (AC0 lo—lo-hi—hi 407819R42185 Hs.102720 ESTs lo—lo-hi—hi 435876 AW612586 Hs.160271 Gprotein-coupled receptor 48 lo—lo-hi—hi 436716 AI433540 gb: ti69g05.x1NCI_CGAP_Kid11 Homo sapien lo—lo-hi—hi 401419 Target Exon lo—lo-hi—hi424363 AW512144 Hs.346947 ESTs, Weakly similar to A48809 carboxylelo—lo-hi—hi 408866 AW292096 Hs.255036 ESTs lo—lo-hi—hi 415516 F11411 gb:HSC2WF081 normalized infant brain cDN lo—lo-hi—hi 423144 AW851527Hs.253677 ESTs, Weakly similar, to I38022 hypotheti lo—lo-hi—hi 452560BE077084 Hs.99969 ESTs lo—lo-hi—hi 439827 AA846538 Hs.187389 ESTslo—lo-hi—hi 419709 AA255592 Hs.347973 ESTs, Weakly similar toalternatively sp lo—lo-hi—hi 413672 BE156536 gb:QV0-HT0368-310100-091-h10 HT0368 Homo lo—lo-hi—hi 425291 AA354572 gb:EST62857 Jurkat T-cells V Homo sapien lo—lo-hi—hi 427403 AA402107Hs.257146 ESTs, Moderately similar to I38022 hypot lo—lo-hi—hi 436911AW937461 Hs.255377 ESTs lo—lo-hi—hi 435293 AI040777 Hs.117170 ESTslo—lo-hi—hi 448490 AI523897 Hs.271692 ESTs, Weakly similar to I38022hypotheti lo—lo-hi—hi 449539 W80363 Hs.58446 ESTs lo—lo-hi—hi 458082AW978611 Hs.314451 ESTs, Weakly similar ALU1_HUMAN ALU S lo—lo-hi—hi459407 N92114 gb: za22h11.r1 Soares fetal liver spleen lo—lo-hi—hi423231 AA323486 Hs.271273 Homo sapiens cDNA FLJ12335 fis, clone MAlo—lo-hi—hi 450628 AW382884 Hs.204715 ESTs lo—lo-hi—hi 411690 AA669253Hs.136075 RNA, U2 small nuclear lo—lo-hi—hi 414739 U83867 Hs.77196spectrin, alpha, non-erythrocytic 1 (alp lo—lo-hi—hi 444169 AV648170Hs.58756 ESTs lo—lo-hi—hi 420911 U77413 Hs.100293 O-linkedN-acetytglusosamine (GlcNAC) tr lo—lo-hi—hi 422195 AB007903 Hs.113082KIAA0443 gene product lo—lo-hi—hi 452704 AA027823 Hs.149424 Homo sapiensPNAS-130 mRNA, complete cds lo—lo-hi—hi 425074 AA495930 Homo sapienscDNA: FLJ22165 fis, clone H lo—lo-hi—hi 426376 N46752 Hs.302985 ESTslo—lo-hi—hi 447754 AW073310 Hs.163533 Homo sapiens cDNA FLJ14142 fis,clone MA lo—lo-hi—hi 413686 AI469213 Hs.71404 ESTs lo—lo-hi—hi 449000U69560 Hs.3826 kelch-like protein C3IP1 lo—lo-hi—hi 430064 AK000091Hs.231436 hypothelical protein FLJ20084 lo—lo-hi—hi 412205 N33818Hs.20274 ESTs, Weakly similar to unnamed protein lo—lo-hi—hi 423955AI420582 Hs.136164 cutaneous T-cell lymphoma-associated turn lo—lo-hi—hi455619 BE063853 gb: QV3-BT0296-011299-022-g09 BT0296 Homo lo—lo-hi—hi408722 AA487860 Hs.298102 ESTs lo—lo-hi—hi 459710 AI701596 Hs.121592ESTs lo—lo-hi—hi 417918 AA209205 Hs.163754 hypothetical protein FLJ12606lo—lo-hi—hi 402964 NM_022095*: Homo sapiens hypothetical C2H lo—lo-hi—hi424387 AI739312 Hs.284163 ANKHZN protein lo—lo-hi—hi 427220 AF069517Hs.173993 RNA binding motif protein 6 lo—lo-hi—hi 410451 BE065687 gb:RC3-BT0316-270400-016-f10 BT0316 Homo lo—lo-hi—hi 400713 NM_006165*:Homo sapiens nuclear factor r lo—lo-hi—hi 407218 AA095473 Hs.28505ubiquitin-conjugating enzyme E2H (homolo lo—lo-hi—hi 449312 N71673Hs.223666 ESTs lo—lo-hi—hi 419612 AI498267 Hs.110613 KIAA0421 proteinlo—lo-hi—hi 455272 BE148152 gb: RC4-HT0231-041199-012-b04 HT0231 Homolo—lo-hi—hi 401839 NM_005177*: Homo sapiens ATPase, H+ trans lo—lo-hi—hi440422 AW452696 Hs.130760 myosin phosphatase, target subunit 2lo—lo-hi—hi 436819 AA731746 Hs.120232 ESTs lo—lo-hi—hi 413644 BE154910Hs.278793 ESTs, Weakly similar to Z195_HUMAN ZINC lo—lo-hi—hi 413939AL047051 Hs.199961 ESTs, Weakly similar to ALU7_HUMAN ALU S lo—lo-hi—hi448198 BE622100 Hs.209406 ESTs, Weakly similar to I38600 zinc finglo—lo-hi—hi 450488 AA009999 Hs.59159 ESTs, Moderately similar to HPV16E1 pro lo—lo-hi—hi 433507 AI817336 Hs.191791 ESTs lo—lo-hi-lo 438996AW748336 Hs.110613 KIAA0421 protein lo—lo-hi-lo 442789 AW904361Hs.131191 ESTs, Weakly similar to ALU7_HUMAN ALU S lo—lo-hi-lo 407251U67611 transaldolase 1 lo—lo-hi-lo 409051 AA080912 gb: zn04d03.r1Stratagene hNT neuron (937 lo—lo-hi-lo 409123 AA063403 gb: zm04d12.s1Stratagene corneal stroma lo—lo-hi-lo 416225 AA577730 Hs.188684 ESTs,Weakly similar to PC4259 ferritin lo—lo-hi-lo 433735 AA608955 Hs.109653ESTs lo—lo-hi-lo 434404 AW445034 Hs.256578 ESTs lo—lo-hi-lo 446667BE161878 Hs.224805 ESTs lo—lo-hi-lo 447982 H22953 Hs.137551 ESTslo—lo-hi-lo 438890 AA827756 Hs.135049 ESTs, Weakly similar to ALU7_HUMANALU S lo—lo-hi-lo 427882 AA640987 Hs.193767 ESTs lo—lo-hi-lo 459680H96982 Hs.42321 ESTs lo—lo-hi-lo 416632 H69480 Hs.141304 ESTslo—lo-hi-lo 453876 AW021748 Hs.110406 ESTs, Weakly similar to I38022hypotheti lo—lo-hi-lo 414528 AA148950 Hs.188836 ESTs lo—lo-hi-lo 419902AA804409 Hs.118920 ESTs lo—lo-hi-lo 409542 AA503020 Hs.36563hypothetical protein FLJ22418 lo—lo-hi-lo 433560 AI925195 Hs.130891hypothetical protein MGC4400 lo—lo-hi-lo 447499 AW262580 Hs.147674protocadherin beta 16 lo—lo-hi-lo 435023 AI692552 gb: wd73f12.x1NCl_CGAP_Lu24 Homo sapiens lo—lo-hi-lo 412156 H29487 Hs.17110 Homosapiens mRNA: cDNA DKFZp434C2016 (f lo—lo-hi-lo 414505 R45389 Hs.23558ESTs, Weakly similar to A8042 lysosomal lo—lo-hi-lo 404277 NM_019111*:Homo sapiens major histocompa lo—lo-hi-lo 414662 AL036058 Hs.76807 majorhistocompatibility complex, class lo—lo-hi-lo 444430 AI611153 Hs.6093Homo sapiens cDNA: FLJ22783 fis, clone K lo—lo-hi-lo 445612 N94126Hs.12969 hypothetical protein lo—lo-hi-lo 403739 ENSP00000251563*:UDP-glucuronosyltransfe lo—lo-hi-lo 403740 NM_001076*: Homo sapiens UDPglycosyltran lo—lo-hi-lo 411084 T18987 Hs.125472 ESTs, Moderatelysimilar to KIAA0877 pro lo—lo-hi-lo 429143 AA333327 Hs.197335 plasmaglutamate carboxypeptidase lo—lo-hi-lo 443060 D78874 Hs.8944 procollagenC-endopeptidase enhancer 2 lo—lo-hi-lo 422749 W01076 Hs.278573 CD59antigen p18-20 (antigen identified lo—lo-hi-lo 429441 AJ224172 Hs.204096lipophilin B (uteroglobin family member) lo—lo-hi-lo 414382 AW380339Hs.8068 hematopoietic PBX-interacting protein lo—lo-hi-lo 441560 F13386Hs.7888 Homo sapiens clone 23736 mRNA sequence lo—lo-hi-lo 446106AA377165 Hs.44833 ESTs lo—lo-hi-lo 452239 AW379378 Hs.170121 proteinlyrosine phosphatase, receptor t lo—lo-hi-lo 446874 AW968304 Hs.56156ESTs lo—lo-hi-lo 412795 BE241753 Hs.74592 special AT-rich sequencebinding protein lo—lo-hi-lo 430325 AF004562 Hs.239356 syntaxin bindingprotein 1 lo—lo-hi-lo 426392 AW968324 Hs.17384 ESTs lo—lo-hi-lo 447448BE244285 F-box only protein 29 lo—lo-hi-lo 415743 AA167664 Hs.14333ESTs, Weakly similar to Z195_HUMAN ZINC lo—lo-hi-lo 431607 AB033097Hs.183669 KIAA1271 protein lo—lo-hi-lo 411979 X85134 Hs.72984retinoblastoma-binding protein 5 lo—lo-hi-lo 453620 BE396163 Hs.25005ESTs, Weakly similar to ALU5_HUMAN ALU S lo—lo-hi-lo 431099 Y13367Hs.249235 phosphoinositide-3-kinase, class 2, alph lo—lo-hi-lo 421687AL035306 Hs.106823 hypothetical protein MGC14797 lo—lo-hi-lo 439565AF086386 Hs.145599 ESTs lo—lo-hi-lo 442349 W40516 Hs.132355 Homo sapienscDNA: FLJ22119 fis, clone H lo—lo-hi-lo 410096 AW245200 Hs.267400hypothetical protein MGC5540 lo—lo-hi-lo 429447 AW812452 Hs.83286 ESTs,Weakly similar to S14747 sphingomy lo—lo-hi-lo 431802 AL133570 Hs.270571Home sapiens mRNA; cDNA DKFZp434L201 (fr lo—lo-hi-lo 441715 AI929453Hs.342655 Homo sapiens cDNA FLJ13289 fis, clone OV lo—lo-hi-lo 458230BE311851 Hs.6639 KIAA1624 protein lo—lo-hi-lo 428788 AF082283 Hs.193516B-cell CLL/lymphoma 10 lo—lo-hi-lo 450818 AI740573 Hs.142827 P311protein lo—lo-hi-lo 419576 AK002060 Hs.91251 hypothetical proteinFLJ11198 lo—lo-hi-lo 400401 AF159093 Homo sapiens endogenous retrovirusRAN1 lo—lo-hi-lo 427004 AI921573 HS.213107 ESTs lo—lo-hi-lo 401178AA046772 RNA binding motif protein, X chromosome lo—lo-hi-lo 423749U09848 Hs.132390 zinc finger protein 36 (KOX 18) lo—lo-hi-lo 428898AB033070 Hs.194408 KIAA1244 protein lo—lo-hi-lo 458258 AW406546Hs.127971 ESTs lo—lo-hi-lo 429521 BE048708 Hs.50949 ESTs lo—lo-hi-lo402185 Target Exon lo—lo-hi-lo 415961 H10983 Hs.155919 ESTs lo—lo-hi-lo457265 AB023212 Hs.225967 KIAA0995 protein lo—lo-hi-lo 412419 AW948630gb: QV0-FT0001-050500-226-g05 FT0001 Homo lo—lo-hi-lo 438397 AA806478Hs.123206 ESTs lo—lo-hi-lo 440509 BE410132 Hs.134202 ESTs, Weaklysimilar to T17279 hypotheti lo—lo-hi-lo 423895 AA332215 gb: EST36124Embryo, 8 week I Homo sapien lo—lo-hi-lo 400251 NM_004651*: Homo sapiensubiquitin specif lo—lo-hi-lo 445094 AW296163 Hs.147296 ESTs lo—lo-hi-lo432323 AK001409 Hs.274356 hypothetical protein FLJ10547 lo—lo-hi-lo444290 AA262496 gb: zs20f11.r1 NCI_CGAP_GCB1 Homo sapiens lo—lo-hi-lo435803 Z44194 Hs.4994 transducer of ERBB2, 2 lo—lo-hi-lo 436905 N31273Hs.42380 ESTs lo—lo-hi-lo 401849 Target Exon lo—lo-hi-lo 402249C19000553*: gi|12741444|ref|XP_008888.2| lo—lo-hi-lo 406180 AB018249small inducible cytokine subfamily A (Cy lo—lo-hi-lo 448176 AI672546Hs.170507 ESTs lo—lo-hi-lo 409259 AW608930 Hs.52184 hypothetical proteinFLJ20618 lo—lo-hi-lo 457335 AW969834 Hs.303303 ESTs lo—lo-hi-lo 452444BE144022 gb: MR0-HT0165-191199-004-f05 HT0165 Homo lo—lo-hi-lo 405429Target Exon lo—lo-hi-lo 430103 AA465259 gb: aa33b03.r1 NCI_CGAP_GCB1Homo sapiens lo—lo-hi-lo 439944 AA856767 Hs.124623 ESTs lo—lo-hi-lo411283 AW852754 gb: PM1-CT0247-180100-009-c05 CT0247 Homo lo—lo-hi-lo458195 R10085 Hs.130370 ESTs lo—lo-hi-lo 452654 BE004783 gb:MR2-BN0114-270400-004-e11 BN0114 Homo lo—lo-hi-lo 425684 AF000989Hs.159201 thymosin, beta 4, Y chromosome lo—lo-hi-lo 29452 AI949495Hs.133998 Homo sapiens cDNA FLJ13202 fis, clone NT lo—lo-hi-lo 431709AF220185 Hs.267923 uncharacterized hypothalamus protein HT0 lo—lo-hi-lo411701 BE181659 gb: QV1-HT0638-070500-191-g07 HT0636 Homo lo—lo-hi-lo430729 AI572560 Hs.301283 KIAA0793 gene product lo—lo-hi-lo 447476BE293466 Hs.20880 ESTs, Weakly similar to I38022 hypotheti lo—lo-hi-lo450436 AW293661 Hs.131887 ESTs lo—lo-hi-lo 405365 CX001212*:gi|7861932|gb|AAF70445.1| (AF2 lo—lo-hi-lo 419555 AA244416 gb:nc07d11.s1 NCI_CGAP_Pr1 Homo sapiens lo—lo-hi-lo 448103 U90918 Hs.13804hypothetical protein dJ462O23.2 lo—lo-hi-lo 400986 NM_024085*: Homosapiens hypothetical pro lo—lo-hi-lo 424194 BE245833 Hs.169854 gb:TCBAP1E1908 Pediatric pre-B cell acut lo—lo-hi-lo 400210 Eos Controllo—lo-hi-lo 400234 NM_005336: Homo sapiens high density lipo lo—lo-hi-lo400235 NM_005336: Homo sapiens high density lipo lo—lo-hi-lo 405387NM_022170*: Homo sapiens Williams-Beuren lo—lo-hi-lo 433075 NM_002959sortilin 1 lo—lo-hi-lo 406302 C16000922: gi|7499103|pir||T20903 hypothelo—lo-hi-lo 428181 AA423976 gb: zv62h06.s1 Soares_testis_NHT Homo saplo—lo-hi-lo 456629 AW891965 Hs.279789 histone deacetylase 3 lo—lo-hi-lo426940 AA393537 Hs.98347 ESTs, Weakly similar to JC5308 testis-splo—lo-hi-lo 433555 AA535902 Hs.146211 Homo sapiens HERC2P7 pseudogene,partial lo—lo-hi-lo 421431 AA650117 Hs.283107 ESTs lo—lo-hi-lo 448631AI554923 gb: te53h12.x1 Soares_NFL_T_GBC_S1 Homo s lo—lo-hi-lo 433521T66087 Hs.112482 Homo sapiens unknown mRNA sequence lo—lo-hi-lo 407187AA446971 gb: zw85f11.s1 Soares_total_fetus_Nb2HF8_(—) lo—lo-hi-lo 450739AI732707 Hs.116506 ESTs, Weakly similar to ALU7_HUMAN ALU S lo—lo-hi-lo440004 BE397117 Hs.120824 hypothetical protein FLJ21845 lo—lo-hi-lo403947 NM_005032 plastin 3 (T isoform) lo—lo-hi-lo 405529 AW410458chromosome 11 open reading frame2 lo—lo-hi-lo 402163 C19001075*:gi|4567179|gb|AAD23607.1|AC00 lo—lo-hi-lo 404663 ENSP00000251884:KIAA1521 protein (Fragme lo—lo-hi-lo 400220 Eos Control lo—lo-hi-lo401444 Target Exon lo—lo-hi-lo 455824 BE143703 gb:MR0-HT0164-191199-004-f03 HT0164 Homo lo—lo-hi-lo 400206 Eos Controllo—lo-hi-lo 458659 AW749895 Hs.332520 Homo sapiens mRNA; cDNADKFZp434A1014 (f lo—lo-hi-lo 428866 AL080190 Hs.189242 Homo sapiensmRNA4; cDNA DKFZp434A202 (fr lo—lo-hi-lo 428442 AA428638 Hs.98606 ESTslo—lo-hi-lo 440151 AA868167 gb: ak38e07.s1 Soares_testis_NHT Homo saplo—lo-hi-lo 431046 AW854382 Hs.249126 Home sapiens clone 24894 mRNAsequence lo—lo-hi-lo 443914 AI091173 Hs.222362 ESTs, Weakly similar top40 [H. sapiens] lo—lo-hi-lo 402469 Target Exon lo—lo-hi-lo 418155R45481 Hs.23719 ESTs, Weakly similar to I38022 hypotheti lo—lo-hi-lo446893 AI610818 Hs.7110 ESTs lo—lo-hi-lo 442336 AW340958 Hs.7572 ESTslo—lo-hi-lo 421290 NM_014368 Hs.103137 LIM homeobox protein 6lo—lo-hi-lo 450374 AA397540 Hs.60293 Homo sapiens clone 122482 unknownmRNA lo—lo-hi-lo 402347 Target Exon lo—lo-hi-lo 415184 AA380436Hs.211973 homolog of Yeast RRP4 (ribosomal RNA pro lo—lo-hi-lo 415632U67085 Hs.78524 TcD37 homolog lo—lo-hi-lo 423718 AL119520 Hs.180737 Homosapiens clone 23664 and 23905 mRNA lo—lo-hi-lo 449140 AW013840 Hs.202092ESTs lo—lo-hi-lo 431241 AA496799 Hs.36958 ESTs lo—lo-hi-lo 416631 H69466gb: yr88f07.r1 Soares fetal liver spleen lo—lo-hi-lo 424168 L29277Hs.321677 signal transducer and activator of trans lo—lo-hi-lo 401600BE247275 U5 snRNP-specific protein, 116 kD lo—lo-hi-lo 420588 AF000982Hs.147916 DEAD/H (Asp-Glu-Ala-Asp/His) box polypep lo—lo-hi-lo 414111BE047679 Hs.152982 hypothetical protein FLJ13117 lo—lo-hi-lo 417138AA193646 Hs.65771 Homo sapiens chromosome 19, BAC CIT-HSPC lo—lo-hi-lo424318 AA476515 Hs.172723 ESTs lo—lo-hi-lo 455653 BE154075 gb:PM0-HT0339-200400-010-E05 HT0339 Homo lo—lo-hi-lo 451493 H38656 Hs.32854ESTs lo—lo-hi-lo 457015 AA688058 Hs.261544 ESTs lo—lo-hi-lo 403654NM_003071: Homo sapiens SWI/SNF related, lo—lo-hi-lo 435203 AW957127Hs.294027 ESTs lo—lo-hi-lo 409322 BE091159 Hs.22687 ESTs, Moderatelysimilar to unnamed prot lo—lo-hi-lo 437764 AA767795 Hs.166832 ESTslo—lo-hi-lo 432542 AW083920 Hs.16098 claudin 2 lo—lo-hi-lo 436125AA765895 Hs.152895 ESTs lo—lo-hi-lo 403217 AL134878 ribosomal protein,large P2 lo—lo-hi-lo 434023 AI277883 Hs.146141 ESTs lo—lo-hi-lo 442419AI749893 Hs.270532 ESTs, Weakly similar to I38022 hypotheti lo—lo-hi-lo443667 AI129066 Hs.135457 ESTs lo—lo-hi-lo 451445 AA017609 Hs.343449 gb:ze37e01.r1 Soares retina N2b4HR Homo lo—lo-hi-lo 454775 BE160229 gb:QV1-HT0413-090200-062-a12 HT0413 Homo lo—lo-hi-lo 411053 AW815061 gb:CM0-ST0209-271099-082-d10 ST0209 Homo lo—lo-hi-lo 435312 AJ243396Hs.4865 voltage-gated sodium channel beta-3 subu lo—lo-hi-lo 450875AK000724 Hs.301553 karyopherin alpha 6 (importin alpha 7) lo—lo-hi-lo451180 H61899 Hs.171937 steroid dehydrogenase like lo—lo-hi-lo 427327AW501456 Hs.288283 Homo sapiens cDNA: FLJ22355 fis, clone H lo—lo-hi-lo444321 AW204210 Hs.122275 Homo sapiens mRNA; cDNA DKFZp564N1623(flo—lo-hi-lo 405109 N47812 CGI-35 protein lo—lo-hi-lo 450182 AI796400Hs.240767 Human DNA sequence from clone RP1-12G14 lo—lo-hi-lo 424990AU076896 Hs.154095 zinc finger protein 143 (clone pHZ-1) lo—lo-hi-lo428997 AF065391 Hs.194718 zinc finger protein 265 lo—lo-hi-lo 402602NM_021186*: Homo sapiens zona pellucida g lo—lo-hi-lo 428772 AI524039Hs.192524 ESTs lo—lo-hi-lo 423759 AI142358 Hs.184361 ESTs, Moderatelysimilar to ALU7_HUMAN A lo—lo-hi-lo 434350 AL042940 Hs.93872 KIAA1682protein lo—lo-hi-lo 442274 AI733484 Hs.129182 ESTs lo—lo-hi-lo 442884AI076570 Hs.134053 ESTs lo—lo-hi-lo 400481 Target Exon lo—lo-hi-lo407283 T51008 gb: yb55e08.s1 Stratagene ovary (937217) lo—lo-hi-lo408859 AW291672 Hs.258981 ESTs lo—lo-hi-lo 455615 BE045344 Hs.274923ESTs, Moderately similar to unnamed prot lo—lo-hi-lo 427315 AA179949Hs.175563 Homo sapiens mRNA; cDNA DKFZp564N0763 (f lo—lo-hi-lo 449375R07114 Hs.271224 ESTs lo—lo-hi-lo 419937 AB040959 Hs.93836 DKFZP434N014protein lo—lo-hi-lo 422231 AA443512 Hs.101383 ESTs lo—lo-hi-lo 437210AA311443 Hs.293563 Homo sapiens mRNA; cDNA DKFZp586E2317 (f lo—lo-hi-lo418056 AA524886 gb: nh34f02.s1 NCI_CGAP_Pr3 Homo sapiens lo—lo-hi-lo446586 N58790 Hs.268820 ESTs lo—lo-hi-lo 407949 W21874 Hs.247057 ESTs,Weakly similar to 2109260A B cell lo—lo-hi-lo 440296 D30829 Hs.180610splicing factor proline/glutamine rich ( lo—lo-hi-lo 422260 AA315993Hs.105484 regenerating gene type IV lo—lo-hi-lo 434685 AA642445Hs.287467 Homo sapiens cDNA FLJ11948 fis, clone HE lo—lo-hi-lo 412657AW976165 gb: EST388274 MAGE resequences, MAGN Homo lo—lo-hi-lo 405188Taget Exon lo—lo-hi-lo 416954 AI222358 gb: qh04c12.x1Soares_NFL_T_GBC_S1 Homo s lo—lo-hi-lo 423700 AA232375 Hs.58606 SNRPNupstream reading frame lo—lo-hi-lo 430288 BE394943 Hs.13804 hypotheticalprotein dJ462O23.2 lo—lo-hi-lo 435184 T67162 Hs.135127 ESTs, Weaklysimilar to unnamed protein lo—lo-hi-lo 431475 AI567669 Hs.40342 putativenuclear protein lo—lo-hi-lo 445239 AI217375 Hs.170023 ESTs, Weaklysimilar to CA36_HUMAN COLLA lo—lo-hi-lo 436151 AK000801 Hs.324271 Homosapiens cDNA FLJ20794 fis, clone CO lo—lo-hi-lo 448489 AI523875 gb:tg97d04.x1 NCI_CGAP_CLL1 Homo sapiens lo—lo-hi-lo 424470 BE244261Hs.323502 Homo sapiens cDNA: FLJ23539 fis, clone L lo—lo-hi-lo 434733AI334367 Hs.159337 ESTs lo—lo-hi-lo 409469 AW517236 Hs.335762 ESTslo—lo-hi-lo 414034 U89277 Hs.305985 early development regulator 1(homolog o lo—lo-hi-lo 420382 AW959165 Hs.270034 Homo sapiens, Similarto nuclear localiz lo—lo-hi-lo 430433 AA478883 Hs.273766 ESTslo—lo-hi-lo 435351 T80177 Hs.118064 similar to rat nuclear ubiquitouscasein lo—lo-hi-lo 403218 AL134878 ribosomal protein, large P2lo—lo-hi-lo 420678 AW593288 Hs.3530 TLS-associated serine-arginineprotein 2 lo—lo-hi-lo 445808 AV655234 ESTs, Moderately similar to PC4259ferri lo—lo-hi-lo 429933 AA765596 Hs.187691 ESTs lo—lo-hi-lo 419802AA250950 Hs.154334 ESTs lo—lo-hi-lo 425155 W26522 Hs.75890 gb: 32g2Human retina cDNA randomly prime lo—lo-hi-lo 417314 N68168 gb:za11c01.s1 Soares fetal liver spleen lo—lo-hi-lo 428290 AI932995Hs.183475 Homo sapiens clone 25061 mRNA sequence lo—lo-hi-lo 422128AW881145 gb: QV0-OT0033-010400-182-a07 OT10033 Homo lo—lo-hi-lo 432014H66741 Hs.38540 ESTs, Weakly similar to ALU4_HUMAN ALU S lo—lo-hi-lo407351 AW383165 gb: PM3-HT0344-151299-004-f07 HT0344 Homo lo—lo-hi-lo443231 W87548 Hs.132932 ESTs lo—lo-hi-lo 444001 AI095087 Hs.152299 ESTs,Moderately similar to S65857 alpha lo—lo-hi-lo 435064 T70740 Hs.31433ESTs lo—lo-hi-lo 435173 AW295645 Hs.255451 ESTs lo—lo-hi-lo 411831AW994394 gb: RC3-BN0036-060400-014-h12 BN0036 Homo lo—lo-hi-lo 446572AV659151 Hs.282961 ESTs lo—lo-hi-lo 428114 AI821548 Hs.98363 ESTs,Weakly similar to I38022 hypotheti lo—lo-hi-lo 406207 Target Exonlo—lo-hi-lo 405011 Target Exon lo—lo-hi-lo 409451 AF012626 Hs.54472fragile X mental retardation 2 lo—lo-hi-lo 411233 AW833793 gb:QV4-TT0008-130100-080-a06 TT0008 Homo lo—lo-hi-lo 455729 BE072092 gb:PM4-BT0532-160200-003-b11 B10532 Homo lo—lo-hi-lo 439454 AA836120Hs.258958 ESTs lo—lo-hi-lo 445124 AI806403 Hs.143942 ESTs lo—lo-hi-lo410324 AW292539 Hs.30177 ESTs lo—lo-hi-lo 446548 AI769392 Hs.200215 ESTslo—lo-hi-lo 416999 AW195747 Hs.21122 hypothetical protein FLJ11830similar to lo—lo-hi-lo 414553 AI813865 Hs.164478 hypothetical proteinFLJ21939 similar to lo—lo-hi-lo 444647 H14718 Hs.11506 Human clone 23589mRNA sequence lo—lo-hi-lo 418271 NM_000919 Hs.83920 peptidylglycinealpha-amidating monooxyg lo—lo-hi-lo 407939 W05608 Hs.312679 ESTs,Weakly similar to A49019 dynein he lo—lo-hi-lo 432676 AI187366 gb:qf29c01.x1 Soares_testis_NHT Homo sap lo—lo-hi-lo 415156 X84908 Hs.78060phosphorylase kinase, beta lo—lo-hi-lo 432679 AI146956 Hs.146723 ESTs,Weakly similar to A53950 transcrip lo—lo-hi-lo 412121 AB033061 Hs.73287KIAA1235 protein lo—lo-hi-lo 418858 AW961605 Hs.21145 hypotheticalprotein RG083M05.2 lo—lo-hi-lo 425204 NM_002436 Hs.1861 membraneprotein, palmitoylated 1 (55 kD) lo—lo-hi-lo 418348 AI537167 Hs.96322hypothetical protein FLJ23560 lo—lo-hi-lo 410765 AI694972 Hs.66180nucleosome assembly protein 1-like 2 lo—lo-hi-lo 445594 AW058463Hs.12940 zinc-fingers and homeoboxes 1 lo—lo-hi-lo 416503 H98502Hs.269853 ESTs lo—lo-hi-lo 426167 AF039023 Hs.167496 RAN binding protein6 lo—lo-hi-lo 451752 AB032997 Hs.26966 KIAA1171 protein lo—lo-hi-lo447124 AW976438 Hs.17428 RBP1-like protein lo—lo-hi-lo 419872 AI422951Hs.146162 ESTs lo—lo-hi-lo 443161 AI038316 gb: ox48c08.x1Soares_total_fetus_Nb2HF8_(—) lo—lo-hi-lo 445391 T92576 Hs.191168 ESTslo—lo-hi-lo 443801 AW206942 Hs.253594 intron of: trichorhinophalangealsyndro lo—lo-hi-lo 446706 AW807631 Hs.190488 Homo sapiens, Similar tonuclear localiz lo—lo-hi-lo 428172 U09367 Hs.182828 zinc finger protein136 (clone pHZ-20) lo—lo-hi-lo 421021 AA808018 Hs.109302 ESTslo—lo-hi-lo 431749 AL049263 Hs.306292 Homo sapiens mRNA; cDNADKFZp564F133 (fr lo—lo-hi-lo 423784 AK000039 Hs.132826 Homo sapiens cDNAFLJ14913 fis, clone PL lo—lo-hi-lo 419479 AI288348 Hs.23450mitochondrial ribosomal protein S25 lo—lo-hi-lo 450900 H61005 Hs.37902ESTs lo—lo-hi-lo 423396 AI382555 Hs.127950 bromodomain-containing 1lo—lo-hi-lo 426137 AL040683 Hs.167031 DKFZP566D133 protein lo—lo-hi-lo442012 AI733277 Hs.128321 ESTs lo—lo-hi-lo 452271 AA025976 Hs.34569 ESTslo—lo-hi-lo 414882 D79994 Hs.77546 Homo sapiens cDNA: FLJ21983 fis,clone H lo—lo-hi-lo 432195 AJ243669 Hs.8127 KIAA0144 gene productlo—lo-hi-lo 430217 N47863 Hs.180450 ribosomal protein S24 lo—lo-hi-lo429567 R35606 Hs.326800 Human EST done 53125 mariner transposonlo—lo-hi-lo 438810 AW897846 Hs.6421 hypothetical protein DKFZp761N09121lo—lo-hi-lo 436796 BE515260 Hs.5320 hypothetical protein lo—lo-hi-lo426352 N72324 Hs.55098 ESTs lo—lo-hi-lo 415308 F05251 gb: HSC04H101normalized infant brain cDN lo—lo-hi-lo 420148 U34227 Hs.95361 myosinVIIA (Usher syndrome 10 (autosoma lo—lo-hi-lo 434442 AA737415 Hs.152826ESTs lo—lo-hi-lo 449429 AA054224 Hs.59847 ESTs lo—lo-hi-lo 410245 C17908Hs.194125 ESTs lo—lo-hi-lo 421168 AF182277 Hs.330780 cytochrome P450,subfamily IIB (phenobar lo—lo-hi-lo 436237 R11528 Hs.271968 ESTslo—lo-hi-lo 440668 AI989538 Hs.191074 ESTs lo—lo-hi-lo 422068 AI807519Hs.104520 Homo sapiens cDNA FLJ13694 fis, clone PL lo—lo-hi-lo 410216BE061839 gb: RC1-BT0254-290100-015-a05 BT0254 Homo lo—lo-hi-lo 439437AI207788 Hs.343628 sialyltransferase 4B (beta-galactosidase lo—lo-hi-lo417061 AI675044 Hs.188691 Homo sapiens cDNA FLJ12033 fis, clone HElo—lo-hi-lo 403046 NM_005656*: Homo sapiens transmembrane pr lo—lo-hi-lo404528 AI912555 peptide YY, 2 (seminalplasmin) lo—lo-hi-lo 439734AC005013 Hs.149 cAMP response element-binding protein CR lo—lo-hi-lo452997 N64777 Hs.44656 ESTs lo—lo-hi-lo 403745 ENSP00000226812*:KIAA1494 protein (Fragm lo—lo-hi-lo 411448 AA178955 Hs.271439 ESTs,Weakly similar to I38022 hypotheti lo—lo-hi-lo 422460 AW445014 Hs.197746ESTs lo—lo-hi-lo 404058 Target Exon lo—lo-hi-lo 436184 BE154067Hs.136660 ESTs, Weakly similar to ZN91_HUMAN ZINC lo—lo-hi-lo 427702N76589 Hs.14454 ESTs, Weakly similar to TFIID subunit TA lo—lo-hi-lo440695 AW088363 Hs.246240 ESTs lo—lo-hi-lo 424881 AL119690 Hs.153618HCGVIII-1 protein lo—lo-hi-lo 440573 BE550891 Hs.270624 ESTs lo—lo-hi-lo416659 W22048 Hs.64753 gb: 61A12 Human retina cDNA Tsp509I-cleavlo—lo-hi—hi 436731 AA580691 Hs.180789 S164 protein lo—lo-hi—hi 405102C15001220*: gi|4469558|gb|AAD21311.1|(AF lo—lo-hi—hi 450219 AI826999Hs.224624 ESTs lo—lo-hi—hi 404527 AI912555 peptide YY, 2(seminalplasmin) lo—lo-hi—hi 439158 R60323 Hs.193888 ESTs lo—lo-hi—hi431952 Z70695 Hs.272240 Homo sapiens cDNA FLJ11086 fis, clone PLlo—lo-hi—hi 418584 NM_004606 Hs.1179 TATA box binding protein(TBP)-associate lo—lo-hi—hi 424241 AW995948 Hs.182339 Homo sapienspyruvate dehydrogenase kina lo—lo-hi—hi 410124 AW962229 Hs.128927 Homosapiens cDNA FLJ13903 fis, clone TH lo—lo-hi—hi 435955 AA830515Hs.222917 ESTs lo—lo-hi—hi 424001 W67883 Hs.137476 paternally expressed10 hi—hi-lo—lo 441399 AI630844 Hs.126919 ESTs hi—hi-lo—lo 440184AB002297 Hs.7022 dedicator of cyto-kinesis 3 hi—hi-lo—lo 421996 AW583807Hs.1460 glucagon hi—hi-lo—lo 444252 R21135 Hs.54985 ESTs hi—hi-lo—lo402082 C18000743*: gi|6678363|ref|NP_033416.1|t hi—hi-lo—lo 405396C22000452*: gi|6981522|ref|NP_036781.1|r hi—hi-lo—lo 412457 T32587Hs.170414 paired basic amino acid cleaving system hi—hi-lo—lo 415808R21439 Hs.334578 Homo sapiens, clone IMAGE: 3929520, mRNA hi—hi-lo—lo441494 AW452344 Hs.129977 ESTs hi—hi-lo—lo 437330 AL353944 Hs.50115 Homosapiens mRNA; cDNA DKFZp761J1112 (f hi—hi-lo—lo 452784 BE463857Hs.151258 hypothetical protein FLJ21062 hi—hi-lo—lo 410037 AB020725Hs.58009 KIAA0918 protein hi—hi-lo—lo 449145 AI632122 Hs.198408 ESTshi—hi-lo—lo 452487 AW207659 Hs.6630 Homo sapiens cDNA FLJ13329 fis,clone OV hi—hi-lo—lo 431031 AA830335 Hs.105273 ESTs hi—hi-lo—lo 427209H06509 Hs.92423 KIAA1566 protein hi—hi-lo—lo 434280 BE005398 gb:CM1-BN0116-150400-189-h02 BN0116 Homo hi—hi-lo—lo 418236 AW994005Hs.337534 ESTs hi—hi-lo—lo 429201 X03178 Hs.198246 group-specificcomponent (vitamin D bind hi—hi-lo—lo 416653 AA768553 Hs.193145metallothionein 1E (functional) hi—hi-lo—lo 422501 AA354690 Hs.144967ESTs hi—hi-lo—lo 425087 R62424 Hs.126059 ESTs hi—hi-lo—lo 426798AA385062 Hs.130260 ESTs hi—hi-lo—lo 443798 R07848 Hs.188522 ESTshi—hi-lo—lo 427254 AL121523 Hs.97774 ESTs hi—hi-lo—lo 431657 AI345227Hs.105448 ESTs, Weakly similar to B34087 hypotheti hi—hi-lo—lo 409963AA133590 Hs.250857 calcium/calmodulin-dependent protein kin hi—hi-lo—lo446006 NM_004403 Hs.13530 deafness, autosomal dominant 5 hi—hi-lo—lo418259 AA215404 ESTs hi—hi-lo—lo 410173 AA706017 Hs.119944 ESTshi—hi-lo—lo 436023 T81819 Hs.302251 ESTs hi—hi-lo—lo 448428 AF282874Hs.21201 nectin 3; DKFZP566B0846 protein hi—hi-lo—lo 430665 BE350122Hs.157367 ESTs, Weakly similar to I78885 serine/th hi—hi-lo—lo 432559AW452948 Hs.257631 ESTs hi—hi-lo—lo 451572 AA018556 Hs.268691 ESTs,Moderately similar to ALU2_HUMAN A hi—hi-lo—lo 456032 AW957446 Hs.301711ESTs hi—hi-lo—lo 438209 AL120659 Hs.6111 aryl-hydrocarbon receptornuclear transl hi—hi-lo—lo 438337 AK002058 Hs.6166 hypothetical proteinFLJ11196 hi—hi-lo—lo 431795 AK002088 Hs.270124 Homo sapiens cDNAFLJ11226 fis, clone PL hi—hi-lo—lo 421114 AW975051 Hs.293156 ESTs,Weakly similar to I78885 serine/th hi—hi-lo—lo 431843 AA516420 ESTs,Weakly similar to I38022 hypotheti hi—hi-lo—lo 440948 AW188311 Hs.128619ESTs hi—hi-lo—lo 430105 X70297 Hs.2540 cholinergic receptor, nicotinic,alpha p hi—hi-lo—lo 439046 AA947354 gb: od86e11.s1 NCI_CGAP_Ov2 Homosapiens hi—hi-lo—lo 451491 AI972094 Hs.286221 Homo sapiens cDNA FLJ13741fis, clone PL hi—hi-lo—lo 452789 AW081626 Hs.242561 ESTs hi—hi-lo—lo419829 AI924228 Hs.115185 ESTs, Moderately similar to PC4259 ferrihi—hi-lo—lo 449567 AI990790 Hs.188614 ESTs hi—hi-lo—lo 407787 N21307Hs.13477 ESTs, Weakly similar to 1207289A reverse hi—hi-lo—lo 409091AW970386 Hs.269423 ESTs hi—hi-lo—lo 435354 AA678267 Hs.117115 ESTshi—hi-lo—lo 444809 BE207568 Hs.208219 oculospanin hi—hi-lo—lo 422170AI791949 Hs.112432 anti-Mullerian hormone hi—hi-lo—lo 453582 AW854339Hs.33476 hypothetical protein FLJ11937 hi—hi-lo—lo 435905 AW997484Hs.5003 KIAA0456 protein hi—hi-lo—lo 443884 N20617 Hs.194397 leptinreceptor hi—hi-lo—lo 430027 AB023197 Hs.227743 KIAA0980 proteinhi—hi-lo—lo 432582 AI623817 Hs.168457 ESTs hi—hi-lo—lo 417993 AW963705Hs.301183 molecule possessing ankyrin repeats indu hi—hi-lo—lo 444930BE185536 Hs.301183 molecule possessing ankyrin repeats indu hi—hi-lo—lo427794 AA709186 Hs.99070 ESTs hi—hi-lo—lo 410913 AL050367 Hs.66762 Homosapiens mRNA; cDNA DKFZp564A026 (fr hi—hi-lo—lo 431992 NM_002742 Hs.2891protein kinase C, mu hi—hi-lo—lo 447846 AA324057 Hs.77955 Homo sapienscDNA: FLJ23527 fis, clone L hi—hi-lo—lo 430439 AL133561 DKFZP434B061protein hi—hi-lo—lo 432621 AI298501 Hs.12807 ESTs, Weakly similar toT46428 hypotheti hi—hi-lo—lo 431427 AK000401 Hs.252748 Homo sapiens cDNAFLJ20394 fis, clone KA hi—hi-lo—lo 408872 AI476139 Hs.13921 ESTshi—hi-lo—lo 453200 AA033832 Hs.212433 ESTs hi—hi-lo—lo 411529 AA430348Hs.317596 Homo sapiens cDNA FLJ12927 fis, clone NT hi—hi-lo—lo 414483R25513 Hs.10683 ESTs hi—hi-lo—lo 451273 NM_014811 Hs.26163 KIAA0649 geneproduct hi—hi-lo—lo 437052 AA861697 Hs.120591 ESTs hi—hi-lo—lo 440049R06699 Hs.19769 hypothetical protein MGC4174 hi—hi-lo—lo 429483 AA974832Hs.128708 ESTs hi—hi-lo—lo 411296 BE207307 Hs.10114 growth suppressor 1hi—hi-lo—lo 425188 AK002052 Hs.155071 hypothetical protein FLJ11190hi—hi-lo—lo 436315 BE390513 Hs.27935 hypothetical protein MGC4837hi—hi-lo—lo 400297 AI127076 Hs.306201 hypothetical protein DKFZp564O1278hi—hi-lo—lo 431089 BE041395 ESTs, Weakly similar to unknown proteinhi—hi-lo—lo 418824 AW751661 Hs.53542 choreoacanthocytosis gene; KIAA0986prot hi—hi-lo—lo 449226 AB002365 Hs.23311 KIAA0367 protein hi—hi-lo—lo450149 AW969781 Hs.132863 Zic family member 2 (odd-paired Drosophihi—hi-lo—lo 418443 NM_005239 Hs.85146 v-ets avian erythroblastosis virusE26 o hi—hi-lo—lo 458692 BE549905 Hs.231754 ESTs hi—hi-lo—lo 410102AW248508 Hs.279727 ESTs; homologue of PEM-3 [Ciona savignyi hi—hi-lo—lo451062 AL110125 Hs.25910 Homo sapiens mRNA; cDNA DKFZp564C1416 (fhi—hi-lo—lo 407633 NM_007069 Hs.37189 similar to rat HREV107 hi—hi-lo—lo418941 AA452970 Hs.239527 E1B-55 kDa-associated protein 5 hi—hi-lo—lo407059 X95406 gb: H. sapiens cyclin E gene. hi—hi-lo—lo 455956 BE162704gb: PM1-HT0454-301299-001-d08 HT0454 Homo hi—hi-lo—lo 437763 AA469369Hs.5831 tissue inhibitor of metalloproteinase 1 hi—hi-lo—lo 451404AA460775 Hs.6295 ESTs, Weakly similar to T17248 hypotheti hi—hi-lo—lo428494 AA233439 Hs.184634 hypothetical protein FLJ20005 hi—hi-lo—lo414957 D61283 Hs.45206 ESTs hi—hi-lo—lo 456415 AI734051 Hs.277102 ESTs,Weakly similar to ALU1_HUMAN ALU S hi—hi-lo—lo 400183 Eos Controlhi—hi-lo—lo 400158 ENSP00000244302*: CDNA FLJ11591 fis, clon hi—hi-lo—lo403893 ENSP00000237068*: Protocadherin alpha 6 p hi—hi-lo—lo 423809AI223833 Hs.154483 ESTs hi—hi-lo—lo 400170 Eos Control hi—hi-lo—lo403291 Target Exon hi—hi-lo—lo 422026 U80736 Hs.110826 trinucleotiderepeat containing 9 hi—hi-lo—lo 417130 AW276858 Hs.81256 S100calcium-binding protein A4 (calcium hi—hi-lo—lo 432472 AA548781Hs.136418 ESTs hi—hi-lo—lo 405231 C2001066: gi|10257425|ref|NP_033892.1|CD hi—hi-lo—lo 400141 Eos Control hi—hi-lo—lo 428971 BE278404 Hs.285813hypothetical protein FLJ11807 hi—hi-lo—lo 422390 AW450893 Hs.121830ESTs, Weakly similar to T42682 hypotheti hi—hi-lo—lo 425538 BE270918Hs.164026 Home sapiens, clone IMAGE: 3534875, mRNA, hi—hi-lo—lo 456972AI054347 Hs.2017 ribosomal protein L38 hi—hi-lo—lo 456622 AF205849Hs.107740 Kruppel-like factor 2 (lung) hi—hi-lo—lo 418515 AI568453Hs.19487 ESTs, Weakly similar to CNIH_HUMAN CORNI hi—hi-lo—lo 448439BE613082 Hs.28229 ARG99 protein hi—hi-lo—lo 445418 AW139377 Hs.127179cryptic gene hi—hi-lo—lo 402559 Z23024 Rho GTPase activating protein 1hi—hi-lo—lo 402575 Z23024 Rho GTPase activating protein 1 hi—hi-lo—lo420811 AA807544 ESTs, Weakly similar to B34323 GTP-bindi hi—hi-lo—lo446627 AI973016 Hs.15725 hypothetical protein SBBI48 hi—hi-lo—lo 400247Eos Control hi—hi-lo—lo 430289 AK001952 Hs.238039 hypothetical proteinFLJ11090 hi—hi-lo—lo 400133 Eos Control hi—hi-lo—lo 418816 T29621Hs.88778 carbonyl reductase 1 hi—hi-lo—lo 433579 BE264473 Hs.284297hypothetical protein from EUROIMAGE 1967 hi—hi-lo—lo 401952 Target Exonhi—hi-lo—lo 410349 AW663021 Hs.323445 ESTs, Weakly similar to T2D3_HUMANTRANS hi—hi-lo—lo 417558 AF045229 Hs.82280 regulator of G-proteinsignalling 10 hi—hi-lo—lo 446851 AW007332 Hs.10450 Homo sapiens cDNA:FLJ22063 fis clone H hi—hi-lo—lo 404489 Target Exon hi—hi-lo—lo 405802Target Exon hi—hi-lo—lo 456266 L29073 Hs.198726 cold shock domainprotein A hi—hi-lo—lo 457133 M54968 v-Ki-ras2 Kirsten rat sarcoma 2viral on hi—hi-lo—lo 459330 C16931 gb: C16931 Clontech human aorta polyAmRN hi—hi-lo—lo 433041 BE265848 Hs.289080 colon cancer-associatedprotein Mic1 lo—lo—lo-hi 446545 AI431798 Hs.164192 ESTs, Weakly similarto Y161_HUMAN HYPOT lo—lo—lo-hi 414911 NM_000107 Hs.77602damage-specific DNA binding protein 2 (4 lo—lo—lo-hi 414682 AL021154Hs.76884 inhibitor of DNA binding 3, dominant neg lo—lo—lo-hi 422311AF073515 Hs.114948 cytokine receptor-like factor 1 lo—lo—lo-hi 447329BE090517 ESTs, Moderately similar to ALU8_HUMAN A lo—lo—lo-hi 412942AL120344 Hs.75074 mitogen-activated protein kinase-activat lo—lo—lo-hi420747 BE294407 Hs.99910 phosphofructokinase, platelet lo—lo—lo-hi431912 AI660552 Hs.76549 ESTs, Weakly similar to A56154 Abl substlo—lo—lo-hi 446506 AI123118 Hs.15159 chemokine-like factor,alternatively spl lo—lo—lo-hi 408633 AW963372 Hs.46677 PRO2000 proteinlo—lo—lo-hi 433675 AW977653 Hs.75319 ribonucleotide reductase M2polypeptide hi-lo—lo-hi 424560 AA158727 Hs.150555 protein predicted byclone 23733 hi-lo—lo-hi 425234 AW152225 Hs.165909 ESTs, Weakly similarto I38022 hypotheti hi-lo—lo-hi 439815 AA206079 Hs.6693 hypotheticalprotein FLJ20420 hi-lo—lo-hi 410174 AA306007 Hs.59461 DKFZP434C245protein hi-lo—lo-hi 410442 X73424 Hs.63788 propionyl Coenzyme Acarboxylase, beta p hi-lo—lo-hi 429190 H18650 Hs.92602 ESTs hi-lo—lo-hi423619 T48691 Hs.249159 adrenergic, alpha-2A-, receptor hi-lo—lo-hi433764 AW753676 Hs.39982 ESTs hi-lo—lo-hi 421998 R74441 Hs.117176poly(A)-binding protein, nuclear 1 hi-lo—lo-hi 451593 AF151879 Hs.26706CGI-121 protein hi-lo—lo-hi 452092 BE245374 Hs.27842 hypotheticalprotein FLJ11210 hi-lo—lo-hi 447425 AI963747 Hs.18573 acylphosphatase 1,erythrocyte (common) hi-lo—lo-hi 421654 AW163267 Hs.106469 suppressor ofvar1 (S. cerevisiae) 3-like hi-lo—lo-hi 432502 NM_014641 Hs.277585KIAA0170 gene product hi-lo—lo-hi 429597 NM_003816 Hs.2442 a disintegrinand metalloproteinase doma hi-lo—lo-hi 434203 BE262677 Hs.283558hypothetical protein PRO1855 hi-lo—lo-hi 438461 AW075485 Hs.286049phosphoserine aminotransferase hi-lo—lo-hi 409142 AL136877 Hs.50758 SMC4(structural maintenance of chromoso hi-lo—lo-hi 439574 AI469788Hs.165190 ESTs hi-lo—lo-hi 438182 AW342140 Hs.182545 ESTs, Weaklysimilar to ALU1_HUMAN ALU S hi-lo—lo-hi 449103 T24968 Hs.23038 HSPC071protein hi-lo—lo-hi 421059 AI654133 Hs.30212 thyroid receptorinteracting protein 15 hi-lo—lo-hi 446939 AL133353 Hs.16606 CGI-32protein hi-lo—lo-hi 408576 NM_003542 Hs.46423 H4 histone family, memberG hi-lo—lo-hi 410073 AW408163 Hs.58488 catenin (cadherin-associatedprotein), a hi-lo—lo-hi 450912 AW939251 Hs.25647 v-fos FBJ murineosteosarcoma viral onco hi-lo—lo-hi 434701 AA460479 Hs.321707 KIAA0742protein hi-lo—lo-hi 450455 AL117424 Hs.25035 chloride intracellularchannel 4 hi-lo—lo-hi 451144 AW956103 Hs.61712 pyruvate dehydrogenasekinase, isoenzyme hi-lo—lo-hi 427390 AI432163 Hs.268231 Homo sapienscDNA: FLJ23111 fis, clone L hi-lo—lo-hi 451831 NM_001674 Hs.460activating transcription factor 3 hi-lo—lo-hi 406776 T16206 Hs.237164ESTs, Highly similar to LDHH_HUMAN L-LAC hi-lo—lo-hi 428157 AI738719Hs.198427 hexokinase 2 hi-lo—lo-hi 408096 BE250162 Hs.83765dihydrofolate reductase hi-lo—lo-hi 418203 X54942 Hs.83758 CDC28 proteinkinase 2 hi-lo—lo-hi 449338 H73444 Hs.394 adrenomeduilin hi-lo—lo-hi422082 AA016188 Hs.111244 hypothetical protein hi-lo—lo-hi 407907AI752235 Hs.41270 procollagen-lysine, 2-oxoglutarate 5-dio hi-lo—lo-hi416655 AW968613 Hs.79428 BCL2/adenovirus E1B 19 kD-interacting prohi-lo—lo-hi 419551 AW582256 Hs.91011 anterior gradient 2 (Xenepuslaevis) hom hi-lo—lo-hi 434094 AA305599 Hs.238205 hypothetical proteinPRO2013 hi-lo—lo-hi 443951 F13272 Hs.111334 ferritin, light polypeptidehi-lo—lo-hi 422975 AA347720 Hs.122669 KIAA0264 protein hi-lo—lo-hi430314 AA369601 Hs.239138 pre-B-cell colony-enhancing factor hi-lo—lo-hi412664 AA421404 Hs.346868 nucleolar protein p40; homolog of yeasthi-lo—lo-hi 408089 H59799 Hs.42644 thioredoxin-like hi-lo—lo-hi 409690W45393 Hs.55888 activating transcription factor 7 hi-lo—lo-hi 442332AI693251 Hs.8248 Target CAT hi-lo—lo-hi 408388 AF091086 Hs.44563hypothetical protein hi-lo—lo-hi 441252 AW360901 Hs.183047 hypotheticalprotein MGC4399 hi-lo—lo-hi 433069 X76732 Hs.3164 nucleobindin 2hi-lo—lo-hi 443837 AI984625 Hs.9884 spindle pole body proteinhi-lo—lo-hi 426108 AA622037 Hs.166468 programmed cell death 5hi-lo—lo-hi 441181 AA416925 Hs.121076 peptidylprolyl isomerase(cyclophilin)-I hi-lo—lo-hi 447397 BE247676 Hs.18442 E-1 enzymehi-lo—lo-hi 427505 AA361562 Hs.178761 26S proteasome-associated pad1homolog hi-lo—lo-hi 430287 AW182459 Hs.125759 ESTs, Weakly similar toLEU5_HUMAN LEUKE hi-lo—lo-hi 415857 AA866115 Hs.127797 Homo sapiens cDNAFLJ1381 fis, clone HE hi-lo—lo-hi 423198 M81933 Hs.1634 cell divisioncycle 25A hi-lo—lo-hi 407687 AK002011 Hs.37558 hypothetical proteinFLJ11149 hi-lo—lo-hi 431374 BE258532 Hs.251871 CTP synthase hi-lo—lo-hi413273 U75679 Hs.75257 stem-loop (histone) binding protein hi-lo—lo-hi442799 AI564739 Hs.68505 ESTs hi-lo—lo-hi 443881 R64512 Hs.237146hypothetical protein FLJ12752 hi-lo—lo-hi 416209 AA236776 Hs.79078 MAD2(mitotic arrest deficient, yeast, h hi-lo—lo-hi 421834 BE543205Hs.288771 DKFZP586A0522 protein hi-lo—lo-hi 411263 BE297802 Hs.69360kinesin-like 6 (mitotic centromere-assoc hi-lo—lo-hi 413924 AL119964Hs.75616 seladin-1 hi-lo—lo-hi 450598 AF151076 Hs.25199 hypotheticalprotein hi-lo—lo-hi 439453 BE264974 Hs.6566 thyroid hormone receptorinteractor 13 hi-lo—lo-hi 429612 AF062649 Hs.252587 pituitarytumor-transforming 1 hi-lo—lo-hi 443426 AF098158 Hs.9329 chromosome 20open reading frame 1 hi-lo—lo-hi 452353 C18825 Hs.29191 epithelialmembrane protein 2 hi-lo—lo-hi 419879 Z17805 Hs.93564 Homer, neuronalimmediate early gene, 2 hi-lo—lo-hi 422363 T55979 Hs.115474 replicationfactor C (activator 1) 3 (38 hi-lo—lo-hi 416065 BE267931 Hs.78996proliferating cell nuclear antigen hi-lo—lo-hi 424308 AW975531 Hs.154443minichromosome maintenance deficient (S. hi-lo—lo-hi 447519 U46258Hs.339665 ESTs hi-lo—lo-hi 437679 NM_014214 Hs.5753 inositol(myo)-1(or4)-monophosphatase 2 hi-lo—lo-hi 446636 AC002563 Hs.15767 citron(rho-interacting, serine/threonin hi-lo—lo-hi 422094 AF129535 Hs.272027F-box only protein 5 hi-lo—lo-hi 440334 BE276112 Hs.7165 zinc fingerprotein 259 hi-lo—lo-hi 421921 H83363 Hs.6820 translocase of innermitochondrial membr hi-lo—lo-hi 422938 NM_001809 Hs.1594 centromereprotin A (17 kD) hi-lo—lo-hi 427719 AI393122 Hs.134726 ESTs hi-lo—lo-hi422283 AW411307 Hs.114311 CDC45 (cell division cycle 45, S. cerevishi-lo—lo-hi 424840 D79987 Hs.153479 extra spindle poles, S. cerevisiae,Homo hi-lo—lo-hi 418216 AA662240 Hs.283099 AF15q14 protein hi-lo—lo-hi412140 AA219691 Hs.73625 RAB6 interacting, kinesin-like (rabkineshi-lo—lo-hi 418322 AA284166 Hs.84113 cyclin-dependent kinase inhibitor 3(CDK hi-lo—lo-hi 428479 Y00272 Hs.334562 cell division cycle 2, G1 to Sand G2 to hi-lo—lo-hi 449722 BE280074 Hs.23960 cyclin B1 hi-lo—lo-hi417933 X02308 Hs.82962 thymidylate synthetase hi-lo—lo-hi 433001AF217513 Hs.279905 clone HQ0310 PRO0310p1 hi-lo—lo-hi 413943 AW294416Hs.144687 Homo sapiens cDNA FLJ12981 fis, clone NT hi-lo—lo-hi 424905NM_002497 Hs.153704 NIMA (never in mitosis gene a)-related k hi-lo—lo-hi422765 AW409701 Hs.1578 baculoviral IAP repeat-containing 5 (surhi-lo—lo-hi 425397 J04088 Hs.156346 topoisomerase (DNA) II alpha (170kD) hi-lo—lo-hi 444371 BE540274 Hs.239 forkhead box M1 hi-lo—lo-hi422956 BE545072 Hs.122579 ECT2 protein (Epithelial cell transformihi-lo—lo-hi 444783 AK001468 Hs.62180 anillin (Drosophila Scrapshomolog), act hi-lo—lo-hi 453884 AA355925 Hs.36232 KIAA0186 gene producthi-lo—lo-hi 416980 AA381133 Hs.80684 high-mobility group (nonhistonechromoso hi-lo—lo-hi 442432 BE093589 Hs.38178 hypothetical proteinFLJ23468 hi-lo—lo-hi 417308 H60720 Hs.81892 KIAA0101 gene producthi-lo—lo-hi 433133 AB027249 Hs.104741 PDZ-binding kinase; T-celloriginated pr hi-lo—lo-hi 432626 AA471098 Hs.278544 acetyl-Coenzyme Aacetyltransferase 2 (a hi-lo—lo-hi 441020 W79283 Hs.35962 ESTshi-lo—lo-hi 412281 AI810054 Hs.14119 ESTs hi-lo—lo-hi 435602 AF217515Hs.283532 uncharacterized bone marrow protein BM03 hi-lo—lo-hi 400882Target Exon hi-lo—lo-hi 446269 AW263155 Hs.14559 hypothetical proteinFLJ10540 hi-lo—lo-hi 417847 AI521558 Hs.7331 hypothetical proteinFLJ22316 hi-lo—lo-hi 400881 NM_025080: Homo sapiens hypothetical prothi-lo—lo-hi 419356 AI656166 Hs.7331 hypothetical protein FLJ22316hi-lo—lo-hi 400292 AA250737 Hs.72472 BMP-R1B hi-lo—lo-hi 415539 AI733881Hs.72472 BMP-R1B hi-lo—lo-hi 453935 AI633770 Hs.42572 ESTs hi-lo—lo-hi420005 AW271106 Hs.133294 ESTs hi-lo—lo-hi 428450 NM_014791 Hs.184339KIAA0175 gene product hi-lo—lo-hi 436291 BE568452 Hs.344037 proteinregulator of cytokinesis 1 hi-lo—lo-hi 441362 BE614410 Hs.23044 RAD51(S. cerevisiae) homolog (E coli Re hi-lo—lo-hi 428484 AF104032 Hs.184601solute carrier family 7 (cationic amino hi-lo—lo-hi 418526 BE019020Hs.85838 solute carrier family 16 (monocarboxylic hi-lo—lo-hi 458809AW972512 Hs.20985 sin3-associated polypeptide, 30 kD hi-lo—lo-hi 444984H15474 Hs.132898 fatty acid desaturase 1 hi-lo—lo-hi 447342 AI199268Hs.19322 Homo sapiens, Similar to RIKEN cDNA 2010 hi-lo—lo-hi 428330L22524 Hs.2256 matrix metalloproteinase 7 (matrilysin, hi-lo—lo-hi428336 AA503115 Hs.183752 microseminoprotein, beta- hi-lo—lo-hi 430389AL117429 Hs.240845 DKFZP434D146 protein hi-lo—lo-hi 417318 AW953937Hs.240845 ESTs hi-lo—lo-hi 422545 X02761 Hs.287820 fibronectin 1hi-lo—lo-hi 417640 D30857 Hs.82353 protein C receptor, endothelial(EPCR) hi-lo—lo-hi 422809 AK001379 Hs.121028 hypothetical proteinFLJ10549 hi-lo—lo-hi 425580 L11144 Hs.1907 galanin hi-lo—lo-hi 416836D54745 Hs.80247 cholecystokinin hi-lo—lo-hi 434170 AA626509 Hs.122329ESTs hi-lo—lo-hi 427958 AA418000 Hs.98280 potassium intermediate/smallconductance hi-lo—lo-hi 439706 AW872527 Hs.59761 ESTs, Weakly similar toDAP1_HUMAN DEATH hi-lo—lo-hi 450088 AW292933 Hs.254110 ESTs hi-lo—lo-hi414219 W20010 Hs.75823 ALL1-fused gene from chromosome 1q hi-lo—lo-hi419201 M22324 Hs.1239 alanyl (membrane) aminopeptidase (aminophi-lo—lo-hi 426263 AI908774 Hs.259785 carnitine palmitoyltransferase I,liver hi-lo—lo-hi 456236 AF045229 Hs.82280 regulator of G-proteinsignalling 10 hi-lo—lo-hi 456607 AI660190 Hs.106070 cyclin-dependentkinase inhibitor 1C (p5 hi-lo—lo-hi 408437 AW957744 Hs.278469 lacrimalproline rich protein hi-lo—lo-hi 421180 BE410992 Hs.258730heme-regulated initiation factor 2-alpha hi-lo—lo-hi 413437 BE313164Hs.75361 gene from NF2/meningioma region of 22q12 hi-lo—lo-hi 432415T16971 Hs.289014 ESTs, Weakly similar to A43932 mucin 2 p hi-lo—lo-hi449230 BE613348 Hs.211579 melanoma cell adhesion molecule hi-lo—lo-hi417979 AU077284 Hs.83081 GTP cyclohydrolase I feedback regulatoryhi-lo—lo-hi 421877 AW250380 Hs.109059 mitochondrial ribosomal proteinL12 hi-lo—lo-hi 412482 AI499930 Hs.334885 mitochondrial GTP bindingprotein hi-lo—lo-hi 428423 AU076517 Hs.184276 solute carrier family 9(sodium/hydrogen hi-lo—lo-hi 422947 AA306782 Hs.122552 G-2 and S-phaseexpressed 1 hi-lo—lo-hi 441072 AW275480 Hs.39504 hypothetical proteinMGC4308 hi-lo—lo-hi 415938 BE383507 Hs.78921 A kinase (PRKA) anchorprotein 1 hi-lo—lo-hi 432278 AL137506 Hs.274256 hypothetical proteinFLJ23563 hi-lo—lo-hi 446651 AA393907 Hs.97179 ESTs hi-lo—lo-hi 431515NM_012152 Hs.258583 endothelial differentiation, lysophospha hi-lo—lo-hi445345 AW003850 Hs.12532 chromosome 1 open reading frame 21 hi-lo—lo-hi458965 AA010319 Hs.60389 ESTs hi-lo—lo-hi 438321 AA576635 Hs.6153 CGI-48protein hi-lo—lo-hi 416783 AA206186 Hs.79889 monocyte to macrophagedifferentiation-a hi-lo—lo-hi 453563 AW608906 Hs.181163 hypotheticalprotein MGC5629 hi-lo—lo-hi 432393 AW205863 Hs.133988 hypotheticalprotein FKSG28 hi-lo—lo-hi 433914 AF108138 Hs.112160 Homo sapiens DNAhelicase homolog (PIF1) hi-lo—lo-hi 414907 X90725 Hs.77597 polo(Drosophia)-like kinase hi-lo—lo-hi 432375 BE536069 Hs.2962 S100calcium-binding protein P hi-lo—lo-hi 440773 AA352702 Hs.37747 Homosapiens, Similar to RIKEN cDNA 2700 hi-lo—lo-hi 415994 NM_002923Hs.78944 regulator of G-protein signalling 2, 24k hi-lo—lo-hi 412722AI343300 Hs.15091 ESTs hi-lo—lo-hi 446839 BE091926 Hs.16244 mitoticspindle coiled-coil related prot hi-lo—lo-hi 428862 NM_000346 Hs.2316SRY (sex determining region Y)-box 9 (ca hi-lo—lo-hi 439108 AW163034Hs.6467 synaptogyrin 3 hi-lo—lo-hi 430178 AW449612 Hs.152475 ESTshi-lo—lo-hi 421733 AL119671 Hs.1420 fibroblast growth factor receptor 3(ach hi-lo—lo-hi 452410 AL133619 Homo sapiens mRNA; cDNA DKFZp434E2321(f hi-lo—lo-hi 430132 AA204686 Hs.234149 hypothetical protein FLJ20647hi-lo—lo-hi 428297 AA236291 Hs.183583 serine (or cysteine) proteinaseinhibito hi-lo—lo-hi 413142 M81740 Hs.75212 ornithine decarboxylase 1hi-lo—lo-hi 427239 BE270447 Hs.174070 ubiquitin carrier proteinhi-lo—lo-hi 409738 BE222975 Hs.56205 insulin induced gene 1 hi-lo—lo-hi410748 BE383816 Hs.12532 chromosome 1 open reading frame 21 hi-lo—lo-hi424506 AF220490 Hs.149623 group III secreted phospholipase A2hi-lo—lo-hi 447333 BE090580 Hs.70704 hypothetical protein dJ616B8.3hi-lo—lo-hi 414761 AU077228 Hs.77256 enhancer of zeste (Drosophila)homolog 2 hi-lo—lo-hi 419602 AW248434 Hs.91521 hypothetical proteinhi-lo—lo-hi 411669 BE612676 Hs.303116 stromal cell-derived factor 2-like1 hi-lo—lo-hi 452322 BE566343 Hs.28988 glutaredoxin (thioltransferase)hi-lo—lo-hi 426006 R49031 Hs.22627 ESTs hi-lo—lo-hi 457465 AW301344Hs.122908 DNA replication factor hi-lo—lo-hi 406867 AA157857 Hs.182265keratin 19 hi-lo—lo-hi 407230 AA157857 Hs.182265 keratin 19 hi-lo—lo-hi446681 AJ003624 Hs.15896 kendrin hi-lo—lo-hi 408493 BE206854 Hs.46039phosphoglycerate mutase 2 (muscle) hi-lo—lo-hi 439186 AI697274 Hs.105435GDP-mannose 4,6-dehydratase hi-lo—lo-hi 424544 M88700 Hs.150403 dopedecarboxylase (aromatic L-amino aci hi-lo—lo-hi 431325 AW026751 Hs.5794ESTs, Weatly similar to 2109260A B cell hi-lo—lo-hi 414922 D00723Hs.77631 glycine cleavage system protein H (amino hi-lo—lo-hi 438291BE514605 Hs.289092 Homo sapiens cDNA: FLJ22380 fis, clone H hi-lo—lo-hi418574 N28754 M-phase phosphoprotein 9 hi-lo—lo-hi 409342 AU077058Hs.54089 BRCA1 associated RING domain 1 hi-lo—lo-hi 432734 AA837396Hs.263925 LIS1-interacting protein NUDE1, rat Homo hi-lo—lo-hi 436087BE300296 Hs.5054 CGI-133 protein hi-lo—lo-hi 420309 AW043637 Hs.21766ESTs, Weakly similar to ALU5_HUMAN ALU S hi-lo—lo-hi 411619 AI418609Hs.71040 hypothetical protein FLJ20425 hi-lo—lo-hi 424381 AA285249Hs.146329 protein kinase Chk2 hi-lo—lo-hi 442547 AA306997 Hs.217484ESTs, Weakly similar to ALU1_HUMAN ALU S hi-lo—lo-hi 430376 AW292053Hs.12532 chromosome 1 open reading frame 21 hi-lo—lo-hi 434666 AF151103Hs.112259 T cell receptor gamma locus hi-lo—lo-hi 412330 NM_005100Hs.788 A kinase (PRKA) anchor protein (gravin) hi-lo—lo-hi 452123AI267615 Hs.38022 ESTs hi-lo—lo-hi 424893 AW295112 Hs.153648 Homosapiens cDNA FLJ13303 fis, clone OV hi-lo—lo-hi 428057 AI343641Hs.185798 ESTs hi-lo—lo-hi 431566 AF176012 Hs.260720 J domain containingprotein 1 hi-lo—lo-hi 439979 AW600291 Hs.6623 hypothetical proteinFLJ10430 hi-lo—lo-hi 418836 AI655499 Hs.161712 ESTs hi-lo—lo-hi 433757AI949974 Hs.152670 ESTs hi-lo—lo-hi 425236 AW067800 Hs.155223stanniocalcin 2 hi-lo—lo-hi 426215 AW963419 Hs.155223 stanniocalcin 2hi-lo—lo-hiPkey: Unique Eos probeset identifier numberExAccn: Exemplar Accession number, Genbank Accession numberUnigeneID: Unigene numberUnigene Title: Unigene gene titlePattern: Broadly defined expression patterns during androgen withdrawal

TABLE 2B Pkey CAT Number Accession 408660 107294_1 AA525775 AA056342AI538978 AW975281 AA664986 409051 109699_1 AA080912 AA075318 AA083403AA076594 AA078992 AA084926 AA081881 AA113913 AA113892 AA083821 AA134801AA082953 AA070343 AA062835 AA075419 AA063293 AA071252 AA078900 AA062836AW974305 409123 110143_1 AA063403 AA070823 AA070050 410216 1184664_1BE061839 AW859863 AW606085 410451 1204118_1 BE065687 BE065637 AW749002H73690 410498 120611_1 AA355749 AA085520 AW966333 AA340319 BE170936411053 1230446_1 AW815061 H71965 AW815072 AW815048 AW815041 AW815047BE152831 BE152490 BE149043 BE149075 BE149035 BE149067 411233 1236369_1AW833793 AW833799 AW833346 AW833371 AW833795 AW833562 AW833667 AW833377411283 1237666_1 AW852754 AW852897 AW852757 AW852617 BE172755 AW835444411701 1254466_1 BE181659 AW890576 AW857638 411831 1260400_1 AW994394AW865900 AW865905 AW865891 AW866014 AW865898 412419 1293418_1 AW948630AW948626 AW948634 AW948616 AW948627 AW948615 AW948631 AW948605 AW948611AW948610 AW948633 AW948623 AW948628 AW948604 AW948602 AW948607 412492130082_1 AW962604 AA368639 AA112257 412657 1318507_1 AW976165 C04000413351 1363660_1 BE086815 BE086823 R81218 R69229 413509 1374313_1BE145419 BE145433 413672 1382512_1 BE156536 BE156439 BE156700 BE156449BE156653 BE156533 BE156524 BE156670 BE156721 BE156723 415308 1533673_1F05251 R13748 Z44028 H14747 415516 1539185_1 F11411 R15237 Z43915 H20760416508 1597894_1 R39769 T53143 H60012 416631 1605019_1 H69466 H93884N59684 416954 163427_1 AI222358 N73390 D61648 AA243520 AA190953 4173141666649_1 N68168 N69188 N90450 418056 171841_1 AA524886 AW971347AA211537 418259 173388_1 AA215404 AI990909 BE464132 AW271459 N74332AI262061 418574 17690_1 N28754 N28747 AI568146 AI979339 AA322671AA322672 AW955043 AI990326 AA776406 AI016250 AA843678 AW451882 N23137N23129 W70051 AI038748 AA831327 AI925845 AW945895 419555 185884_1AA244416 AA244401 420811 196677_1 AA807544 AA280648 AI243056 AI022744AA705288 AA829425 AW452095 AI929317 R19039 AA282024 421911 208987_1AL041520 AA300086 421974 209807_1 AA301270 AA301379 AA301366 422128211994_1 AW881145 AA490718 M85637 AA304575 T06067 AA331991 423028224062_1 H90946 AA320597 AW954970 BE143680 423476 22861_1 AL035633F11794 F11783 H18042 T66089 H29379 R19493 AW134660 AI299437 AL133995AA057405 N78357 AA917450 AI002692 T09262 T65008 H29290 AI200874 AA894415AI732887 AI791768 AI733447 AA988785 N62128 T09261 AW956936 423895233006_1 AA332215 AA403110 AW965299 424593 241234_1 AA343729 AA345779AA344370 425074 246486_1 AA495930 AI470890 H97831 AA350358 BE166712425291 249618_1 AA354572 AW062361 AW813419 AW816041 AI744949 425980258778_1 AA366951 AA470999 AA469425 426413 266650_1 AA377823 AW954494AI022688 428181 287953_1 AA423976 AA437075 BE006469 429163 300543_1AA884766 AW974271 AA592975 AA447312 429540 305828_1 M85776 AA454535AA456208 H90189 430068 312849_1 AA464964 M85405 AA947566 430103 313089_1AA465259 AW897142 AW897144 430439 31808_1 AL133561 AL041090 AL117481AL122069 AW439292 AI968826 431089 327825_1 BE041395 AA491826 AA621946AA715980 AA666102 431843 338324_1 AA516420 C14818 C14815 C15161 C15068D80763 D60656 AW970134 AA543007 D81004 D60184 AI498371 D60382 D60181C15876 432079 341114_1 AW972746 AA525323 AI150314 432340 345248_1AA534222 AA632632 T81234 432676 352582_2 AI187366 AA558869 AA618478433075 35820_1 NM_002959 X98248 AA233278 AA846376 AI470560 AI470533BE327147 AW291971 AA017125 AI198417 AI365213 AI168442 AI337018 AI475049H86459 AA969895 AA888000 AA418326 AA418378 N71981 AL043634 AA426361AA418275 AA232975 AL036861 BE277220 BE387505 N99710 AW375004 AA418268AL079651 H85743 AW902319 AW805907 AA984366 T92310 AA405425 AA421732AI656841 AW300968 AW593418 T92267 BE464032 AW473548 AI359502 BE552306AI990196 AW518351 AI239559 AW590963 AA018359 AI273737 AL042658 AA411308AA402810 H38111 AW013931 AW366432 AW752435 AW376124 AI292020 AI292121AA340647 BE613672 BE409874 AA351915 BE617026 BE019588 AW402692 AW247466R59233 AA134761 BE254019 BE265105 D63316 BE313080 BE547713 BE536578BE546749 AA324185 H17386 BE253377 R87598 H29072 AA350980 BE076629BE253957 AA532613 BE252486 AW804459 D30966 R87959 AA091832 434280382816_1 BE005398 AA626622 AA994155 434609 38950_1 R76593 AF147390R76594 435023 398093_1 AI692552 AI393343 AI800510 AI377711 F24263AA661876 436716 425440_1 AI433540 AA728984 AA804981 436862 42814_2AI821940 N67106 AI744264 AA808846 AA643417 AA643416 Z70715 43757643892_1 BE514383 AA071273 AW247987 AW673286 BE312102 AW749824 BE071985AW577383 BE071945 BE072005 AW577355 BE071965 AW239231 BE072000 BE071960AW577360 AW749830 AW373020 X97303 AW999522 BE000192 BE562219 BE266655BE264970 438869 46651_1 AF075009 R63109 R63068 438882 466649_1 AA827695AA833754 AW978946 438980 467544_1 AW502384 AI982587 AA828822 439046468133_1 AA947354 AA829660 AI687296 439848 477806_1 AW979249 D63277AA846968 440151 487109_1 AA868167 F21558 F31418 F35624 440507 495677_1H06994 BE147898 441102 509604_1 AA973905 AI299888 AA917019 H63235 T90771442048 531432_1 AA974603 AI984319 AW340495 443161 561305_1 AI038316AI344631 AI261653 444290 59994_1 AA262496 AV648929 AA305356 D61644D78724 444314 600667_1 AI140497 AW749625 AW749626 AW749644 44580865133_1 AV655234 AW966332 AA340239 447329 71759_1 BE090517 AW970792AW264490 AW014985 F27436 AA947336 F15843 H89338 AA563626 F17712 BE546579AA421821 AA284952 AA477751 AW025245 447448 722246_1 BE244285 C18429H42373 AI820706 AI379786 R55439 AW276142 448150 752165_1 AI472167AI990315 R32175 448489 765247_1 AI523875 R45782 R45781 448631 772996_1AI554923 AI902356 448738 77790_1 BE614081 W01988 AW500790 452410 9163_1AL133619 AA468118 AA383064 AI476447 T09430 AI673758 AA524895 AI581345AI300820 AW498812 AA256162 AI559724 AI685732 AA602400 AA905453 AI204595AW166541 AA157456 AA156269 AA383652 AA431072 AW592707 AI435410 AW272464AI215594 AA622747 R74039 N35031 AI804128 AW513621 AA868351 AI026826AI493388 AA614641 W81604 AI567080 AI214351 AA730140 AI125754 AI200813AI269603 AI565082 AI807095 AI476629 AA505909 AI368449 AI686077 AI582930AW085038 AA757863 AA730154 AI767072 AA468316 AI734130 AI734138 AA426284AA433997 AI741241 AW043563 AI732741 AI732734 AA437369 AA425820 AA664048R74130 452444 918078_1 BE144022 BE143969 BE143915 452654 925931_1BE004783 BE004947 AI911790 454775 1234106_1 BE160229 AW819879 AW820179AW819882 AW819876 AW820169 BE153201 AW993736 BE152911 455019 1249138_1AW850818 AW850833 AW851100 455272 1271871_1 BE148152 BE148133 BE148159BE148132 AW885107 455619 1346387_1 BE063853 BE063955 BE063866 BE063705BE063846 BE061416 BE063844 455653 1348742_1 BE154075 BE153973 BE064861BE153852 BE153847 BE064684 BE153602 BE065075 BE154018 BE064772 BE064842BE153557 BE153509 455729 1353792_1 BE072092 BE072106 BE072086 BE072098BE072103 455824 1372880_1 BE143703 BE143631 BE143629 BE143702 4559561387163_1 BE162704 BE162705 BE162732 BE162702 BE162694 456123 1534442_1R00602 Z42921 F06132 457133 29066_1 M54968 NM_004985 AI808924 AL135130AW242010 AA476848 AI740449 M17087 K03210 M35505 M35504 L00049 AI186585W35273 X01669 X02825 W23635 AI554920 AI539465 AA425263 AI469981 W21091T28976 AW977922 BE550180 AW664973 AI148939 AW117295 AA811229 AI343010AA766141 BE219368 N95249 AA280396 AW504574 AA232870 AI770018 AA262948AW450230 AW362890 AW609417 AW499941 AA425857 AW380665 AA830647 AA282180T27356 H85307 AA861543 AA356548 AA356410 AW860656 AW860647 AW938103AW860649 AI567016 N70374 AW474707 AA505084 AA082195 AW949515 AA361728N33863 AA411821 AA401640 AW594461 AL120766 AI500024 AW771891 H84567D51551 AA330460 R14184 AI301629 N64676 AV659669 AI697660 AI004579AA287927 AW453052 AW601642 AA676681 AA737010 AA872481 AA281094 AA564243BE464958 BE049265 AW167917 AA843916 AA525301 AI015987 N25230 AI889481AW173466 AA937541 AI334416 AI676214 AI281159 AA553559 AA582189 AA255527AW160515 AA670007 H08199 AA808271 AA281015 W47527 AA649252 AI364302AA889246 R40473 H02312 AA648116 AA342730 AA243624 R99351 R41588 R49696AA854442 F01713 AA213685 AA721296 R79833 H84241 R70668 H85554 AA223758N95349 AI374913 AI306683 AA015609 AA918548 AI453570 AA772321 AI692775AA195733 AI474563 AW873048 AI209133 AI028182 AI374920 AW572807 AA406223AA833684 T97255 H69138 AA382906 AW119162 N31974 AI890584 N39418 AA864877AA679469 BE350651 N41020 AI050915 F00075 AA864878 N26970 AA828898AW019991 AW796631 AW993262 N48532 BE564662 AV654063 AI754461 AW945712C03289 AV655314 AV659070 AV659808 AV660435 H70113 C05323 R91984 H96949AV658936 AV658879 H69137 AA384411 AA412584 C02749 W32014 R58168 C05526BE536017 N24354 AA287991 N80109 F05452 R12740 H08297 AL138354 AW020801BE178443 BE178018 BE178336 BE178360 BE178107 BE178385 BE178215 BE178186BE178447 BE178352 BE178422 BE178424 BE178043 BE178093 BE178460 BE178356BE178441 BE178438 BE178467 AI091259 BE177839 BE178094 R28455 BE177844BE178100 AA262387 R70669 W80934 W93668 AA256711 BE178141 BE177893BE178449 AA167718 H69694 BE178017 BE178029 BE177999 BE177936 AA095144N32462 AA281203 AA281183 W47526 W05015 R34165 R35306 T97366 R79640W25258 R99450 AW368425 BE178196 R26447 C03146 C03683 457952 44256_1U25750 AI792472 AA487379 AI872282 AA487262 R22383 AI865750 R21832AA593628 AW571869 AA377191 R78814 T27193 458956 83645_1 BE220675AA345621 AA009992Pkey: Unique Eos probeset identifier numberCAT number: Gene cluster numberAccession: Genbank accession numbers

TABLE 2C Pkey Ref Strand Nt_position 400481 8439853 Plus 112433-112541400501 9796227 Minus 12479-12619 400713 8118874 Minus 43185-43394 4007698131628 Plus 28671-29795 400818 8569994 Plus 172644-172765,173085-173200 400881 2842777 Minus 91446-91603, 92123-92265 4008822842777 Minus 110431-110708 400965 7770576 Minus 173043-173564 4009868085497 Minus 63140-63319 400995 8099094 Plus 141186-141601 4010938516137 Minus 22335-23166 401178 9438616 Minus 133663-133812 4011929719502 Minus 69559-70101 401209 7712287 Plus 164932-165112 4014057768126 Minus 69276-69452, 69548-69958 401416 7452889 Minus121456-121626 401419 7452889 Minus 136389-136508 401444 8346725 Plus90895-90994, 93070-93213 401512 7622346 Plus 136399-136557 4015638247910 Plus 91395-91763 401600 4388746 Minus 27363-27518, 28727-28891,29526-29731 401750 9828651 Plus 82143-82270, 89284-89373, 90596-90770,95822-96001, 96688-96775, 96870-96992, 98046-98138 401757 7239630 Plus88641-88751 401839 7656637 Plus 1016-1086, 2751-2967, 3241-3348,26677-26831 401849 7770425 Plus 129375-129483, 129597-129720 4019523319121 Minus 53770-53979 401966 3126781 Plus 29397-29918 402082 8117478Minus 190046-190183 402101 8117697 Plus 134308-134487, 135402-135587,136421-136548 402106 8131652 Plus 3717-3848 402163 8568936 Plus166996-167119 402185 8576002 Plus 25486-25639 402240 7690131 Plus104382-104527, 106136-106372 402249 7704953 Minus 107636-107813,108694-108824, 110435-110502, 113182-113386 402347 8099267 Minus13714-15440 402396 1905896 Plus 4426-4648 402469 9797107 Minus71266-72351 402532 9800951 Minus 180240-180558 402559 9864273 Plus33539-33715 402575 9884830 Minus 109742-109883 402602 7239666 Plus6785-6972, 7478-7575 402758 9213869 Plus 87638-87924 402786 9715046 Plus47624-47795 402807 6456148 Minus 101542-101660, 103476-103656 4028106010110 Plus 12715-12856, 13527-13643 402964 9581599 Minus 46624-46784403046 3540153 Minus 55707-55859, 56369-56511 403055 8748904 Minus109532-110225 403217 7630969 Plus 54089-54163, 55427-55623 4032187630969 Plus 58039-58149 403291 7230870 Plus 95177-95435 403328 8469086Minus 120428-120703 403654 8736093 Minus 28634-28758 403704 4982546Minus 8850-8996 403708 5705981 Minus 134394-134812 403725 7534031 Plus86737-86843 403739 7630882 Plus 44563-44766, 48209-48483, 52255-52495403740 7630882 Plus 86504-87227 403745 7652036 Minus 67610-68002 4037467652036 Plus 93612-93887 403885 7710403 Minus 53259-53524 403893 7710581Minus 5435-7846 403947 7711923 Plus 38657-38817 404039 8698763 Plus81889-82011 404054 3548785 Plus 66713-69175 404058 3548785 Plus99397-101808 404108 8247074 Minus 63603-64942 404211 5006246 Plus185728-185885, 194575-194686 404277 1834458 Minus 91665-91946 4043848887028 Minus 38055-38156, 42175-42391, 43435-43553 404407 7329316 Minus48154-48499 404489 8113772 Plus 98183-98480 404527 8152087 Plus127737-127796, 128080-128210, 129888-130054, 132545-132869 4045288152087 Plus 135325-135486 404661 9797073 Plus 33374-33675, 33769-34008404663 9797133 Plus 29885-30514 404956 7387343 Plus 55883-56203 4050116139150 Plus 117359-117612 405044 7596797 Minus 98903-101141 4051028076881 Minus 120922-121296 405109 8096886 Minus 30301-30518 4051886649489 Plus 134573-134678 405231 7249032 Minus 109793-109969 4053652275192 Minus 119867-120372, 120481-120824, 121029-121357 405387 6587915Minus 3769-3833, 5708-5895 405396 6624129 Minus 89965-90273 4054297321905 Minus 51577-51723 405435 7408068 Minus 51704-51841, 53581-53767405446 7582529 Plus 99136-99313 405503 9211311 Minus 51198-51314 4055259558552 Minus 19699-19828 405529 9581957 Minus 38944-39213 4056105757553 Minus 71907-72080 405802 5924004 Minus 27743-28264 4058114902753 Plus 5128-5248 406180 7283201 Minus 38923-39107 406207 5923650Minus 162607-162800 406302 8575868 Plus 168961-169150, 169610-169769Pkey: Unique number corresponding to an Eos probesetRef: Sequence source. The 7 digit numbers in this column are GenbankIdentifier (GI) numbers. “Dunham I. et al.” refers to the publicationentitled “The DNA sequence of human chromosome 22.” Dunham I. et al.(1999) Nature 402: 489-495.Strand: Indicates DNA strand from which exons were predicted.Nt_position: Indicates nucleotide positions of predicted exons.

Table 3A shows the Seq ID No. Pkey, ExAccn, UnigenID, and Unigene Titlefor all of the sequences in Table 4. Pkey ExAccn UnigeneID Unigene TitleSeq ID No 415539 AI733881 Hs.72472 BMP-R1B Seq ID No 1 & 2 448988 Y09763Hs.22785 gamma-aminobutyric acid (GABA) A recepto Seq ID No 3-10 403740NM_001076*: Homo sapiens UDP glycosyltran Seq ID No 11 & 12 408633AW963372 Hs.46677 PRO2000 protein Seq ID No 13 & 14 408660 AA525775ESTs, Moderately similar to PC4259 ferri Seq ID No 15 & 16 409051AA080912 gb: zn04d03.r1 Stratagene hNT neuron (937 Seq ID No 17 409123AA063403 gb: zm04d12.s1 Stratagene corneal stroma Seq ID No 18 415787H01463 Hs.93534 ESTs Seq ID No 19-21 415999 AA172179 Hs.294029 ESTs SeqID No 22 416225 AA577730 Hs.188684 ESTs, Weakly similar to PC4259ferritin Seq ID No 23 420757 X78592 Hs.99915 androgen receptor(dihydrotestosterone r Seq ID No 24 & 25 429163 AA884766 gb: am20a10.s1Soares_NFL_T_GBC_S1 Homo s Seq ID No 26 429441 AJ224172 Hs.204096lipophilin B (uteroglobin family member) Seq ID No 27 & 28 431099 Y13367Hs.249235 phosphoinositide-3-kinase, class 2, alph Seq ID No 29 & 30432432 AA541323 Hs.115831 ESTs Seq ID No 31 432435 BE218886 Hs.282070ESTs Seq ID No 32 & 33 432527 AW975028 Hs.102754 ESTs Seq ID No 34435876 AW612586 Hs.160271 G protein-coupled receptor 48 Seq ID No 35 &36 438233 W52448 Hs.56147 ESTs Seq ID No 37-40 439569 AW602166 Hs.222399CEGP1 protein Seq ID No 41 & 42 440819 AI809444 Hs.202108 ESTs Seq ID No43 442832 AW206560 Hs.253569 ESTs Seq ID No 44 447342 AI199268 Hs.19322Homo sapiens, Similar to RIKEN cDNA 2010 Seq ID No 45 & 46 447499AW262580 Hs.147674 protocadherin beta 16 Seq ID No 47 & 48 451411AA017492 Hs.135655 EST Seq ID No 49 451720 AW970985 Hs.290853 ESTs SeqID No 50 & 51Pkey: Unique Eos probeset identifier numberExAccn: Exemplar Accession number, Genbank accession numberUnigeneID: Unigene numberUnigene Title: Unigene gene titleSeq ID No: Seq ID number correlation for those sequences in Table 4

Table 3B shows the accession numbers for thos Pkey's lacking UnigeneID'sfor Table 3A. For each probeset is listed gene cluster number from whicholigonucleotides were designed. Gene clusters were compiled usingsequences derived fro Genbank ESTs and mRNAs. These sequences wereclustered based on sequences sililarity using Clustering and AlignmentTools (Double Twist Oakland California). Genebank accession num,bers forsequences comprising each cluster are listed in the “Accession” column.Pkey CAT Number Accession 408660 107294_1 AA525775 AA056342 AI538978AW975281 AA664986 409051 109699_1 AA080912 AA075318 AA083403 AA076594AA078992 AA084926 AA081881 AA113913 AA113892 AA083821 AA134801 AA082953AA070343 AA062835 AA075419 AA063293 AA071252 AA078900 AA062836 AW974305409123 110143_1 AA063403 AA070823 AA070050 429163 300543_1 AA884766AW974271 AA592975 AA447312

Table 3C shows genomic positioning for those Pkey's lacking Unigene ID'sand accession numbers in Table 3A. For each predicated exon is listedgenomic sequence source used for prediction. Nucleotide locations ofeach predicted exon are also listed. Pkey Ref Strand Nt_position 4037407630882 Plus 86504-87227

TABLE 4 Seq ID NO: 1 DNA sequence Nucleic Acid Accession #: NM_001203Coding sequence 274..17821          11         21         31         41         51|          |          |          |          |          | CGCGDGGCGCGGAGTCGGCG GGGCCTCGCG GGACGCGGCC AGTGCGGAGA CCGCGGCCCT 60 GAGGACGCGGGAGCCGGGAG CGCACGCGCG GGGTGGAGTT CAGCCTACTC TTTCTTAGAT 120 GTGAAAGGAAAGGAAGATCA TTTCATGCCT TGTTGATAAA GGTTCAGACT TCTGCTGATT 180 CATAACCATTTGGCTCTGAG CTATGACAAG AGAGGAAACA AAAAGTTAAA CTTACAAGCC 240 TGCCATAAGTGAGAAGCAAA CTTCCTTGAT AACATGCTTT TGCGAAGTGC AGDAAAATTA 300 AATGTGGGCACCAAGAAAGA CCATGGTGAG AGTACAGCCC CCACCCCCCG TCCAAAGGTC 360 TTGCGTTGTAAATGCCACCA CCATTGTCCA GAAGACTCAG TCAACAATAT TTGCAGCACA 420 GACGGATATTGTTTCACGAT GATAGAAGAG GATGACTCTG GGTTGCCTGT GGTCACTTCT 480 GGTTGCCTAGGACTAGAAGG CTCAGATTTT CAGTGTCGGG ACACTCCCAT TCCTCATCAA 640 AGAAGATCAATTGAATGCTG CACAGAAAGG AACGAATGTA ATAAAGACCT ACACCCTACA 600 CTGCCTCCATTGAAAAACAG AGATTTTGTT GATGGACGTA TACACCACAG GGCTTTACTT 660 ATATCTGTGACTGTCTGTAG TTTGCTCTTG GTCCTTATCA TATTATTTTG TTACTTCCGG 720 TATAAAAGACAAGAAACCAG ACCTCGATAC AGCATTGGGT TAGAACAGGA TGAAACTTAC 780 ATTCCTCCTGGAGAATCCCT GAGAGACTTA ATTGAGCAGT CTCAGAGCTC AGGAAGTGGA 840 TCAGGCCTCCCTCTGCTGGT CCAAAGGACT ATAGCTAAGC AGATTCAGAT GGTGAAACAG 900 ATTGGAAAAGGTCGCTATGG GGAAGTTTGG ATGGGAAAGT GGCGTGGCGA AAAGGTAGCT 960 GTGAAAGTGTTCTTCACCAC AGAGGAAGCC AGCTCGTTCA GAGAGACAGA AATATATCAG 1020 ACAGTGTTGATGAGGCATGA AAACATTTTG GGTTTCATTG CTGCAGATAT CAAAGGGACA 1080 GGGTCCTGGACCCAGTTGTA CCTAATCACA GACTATCATG AAAATGGTTC CCTTTATGAT 1140 TATCTGAAGTCCACCACCCT AGACGCTAAA TCAATGCTGA AGTTAGCCTA CTCTTCTGTC 1200 AGTGGCTTATGTCATTTACA CACAGAAATC TTTAGTACTC AAGGCAAACC AGCAATTGCC 1260 CATCGAGATCTGAAAAGTAA AAACATTCTG GTGAAGAAAA ATGGAACTTG CTGTATTGCT 1320 GACCTGGGCCTGGCTGTTAA ATTTATTAGT GATACAAATG AAGTTGACAT ACCACCTAAC 1380 ACTCGAGTTGGCACCAAACG CTATATGCCT CCAGAAGTGT TGGACGAGAG CTTGAACAGA 1440 AATCACTTCCAGTCTTACAT CATGGCTGAC ATGTATAGTT TTGGCCTCAT CCTTTGGGAG 1600 GTTGCTAGGAGATGTGTATC AGGAGGTATA GTGGAAGAAT ACCAGCTTCC TTATCATGAC 1560 CTAGTGCCCAGTGACCCCTC TTATGAGGAC ATGAGGGAGA TTGTGTGCAT CAAGAAGTTA 1620 CGCCCCTCATTCCCAAACCG GTGGAGCAGT GATGAGTGTC TAAGGCAGAT GGGAAAACTC 1680 ATGACAGAATGCTGGGCTCA CAATCCTGCA TCAAGGCTGA CAGCCCTGCG GGTTAAGAAA 1740 ACACTTGCCAAAATGTCAGA GTCCCAGGAC ATTAAACTCT GATAGGAGAG GAAAAGTAAG 1800 CATCTCTGCAGAAAGCCAAC AGGTACTCTT CTGTTTGTGG GCAGAGCAAA AGACATCAAA 1860 TAAGCATCCACAGTACAAGC CTTGAACATC GTCCTGCTTC CCAGTGGGTT CAGACCTCAC 1920 CTTTCAGGGAGCGACCTGGG CAAAGACAGA GAAGCTCCCA GAAGGAGAGA TTGATCCGTG 1380 TCTGTTTGTAGGCGGAGAAA CCGTTGGGTA ACTTGTTCAA GATATGATGC AT Seq ID NO: 2 Proteinsequence Protein Accession #: NP_0011841          11         21         31         41         51|          |          |          |          |          | MLLRSAGKLNVGTKKEDGES TAPTPRPKVL RCKCHHHCPE DSVNNICSTD GYCFTMIEED 60 DSGLPVVTSGCLGLEGSDFQ CRDTPIPHQR RSIECCTERN ECNKDLNPTL PPLKNRDFVD 120 GPIHHRALLISVTVCSLLLV LIILFCYPRY KRQETRPRYS IGLEQDETYI PPGESLRDLI 180 EQSQSSGSGSGLPLLVQRTI AKQIQMVKQI GKGRYGEVWM GKWRGEKVAV KVFFTTEEAS 240 WFRETEIYQTVLMRHEMTLG FIAADIKGTG SWTQLYLITD YHENGSLYDY LKSTTLDAKS 300 MLKLAYSSVSGLGNLHTEIF STQGKPAIAH RDLKSNKILV KKNGTCCIAD LGLAVKFISD 380 TNEVDIPPNTRVGTKRYMPP EVLDESLNRN HFQSYIMADM YSFGLILWEV ARRCVSGGIV 420 EEYQLPYHDLVPSDPSYEDM REIVCIKKLR PSFPNRWSSD ECLRQMGKLM TECWAHNPAS 480 RLTALRVKKTLAKMSESQDI KL Seq ID NO: 3 DNA sequence Nucleic Acid Accession #:NM_004981.2 Coding sequence: 55..15751          11         21         31         41         51|          |          |          |          |          | GCCAGAGCGTGAGCCGCGAC CTCCGCGCAG GTGGTCGCGC CGGTCTCCGC GGAAATGTTG 60 TCCAAAGTTCTTCCAGTCCT CCTAGGCATC TTATTGATCC TCCAGTCGAG GGTCGAGGGA 120 CCTCAGACTGAATCAAAGAA TGAAGCCTCT TCCCGTGATG TTGTCTATGG CCCCCAGCCC 180 CAGCCTCTGGAAAATCAGCT CCTCTCTGAG GAAACAAAGT CAACTGAGAC TGAGACTGGG 240 AGCAGAGTTGGCAAACTGCC AGAAGCCTCT CGCATCCTGA ACACTATCCT GAGTAATTAT 300 GACCACAAACTGCGCCCTGG CATTGGAGAG AAGCCCACTG TGGTCACTGT TGAGATCGCC 360 GTCAACAGCCTTGGTCCTCT CTCTATCCTA GACATGGAAT ACACCATTGA CATCATCTTC 420 TCCCAGACCTGGTACGACGA ACGCCTCTGT TACAACGACA CCTTTGAGTC TCTTGTTCTG 480 AATGGCAATGTGGTGAGCCA GCTATGGATC CCGGACACCT TTTTTAGGAA TTCTAAGAGG 540 ACCCACGAGCATGAGATCAC CATGCCCAAC CAGATGGTCC GCATCTACAA GGATGGCAAG 800 GTGTTGTACACAATTAGGAT GACCATTGAT GCCGGATGCT CACTCCACAT GCTCAGATTT 860 CCAATGGATTCTCACTCTTG CCCTCTATCT TTCTCTAGCT TTTCCTATCC TGAGAATGAG 720 ATGATCTACAAGTGGGAAAA TTTCAAGCTT GAAATCAATG AGAAGAACTC CTGGAAGCTC 780 TTCCAGTTTGATTTTACAGG AGTGAGCAAC AAAACTGAAA TAATCACAAC CCCAGTTGGT 840 GACTTCATGGTCATGACGAT TTTCTTCAAT GTGAGCAGGC GGTTTGGCTA TGTTGCCTTT 900 CAAAACTATGTCCCTTCTTC CGTGACCACG ATGCTCTCCT GGGTTTCCTT TTGGATCAAG 960 ACAGAGTCTGCTCCAGCCCG GACCTCTCTA GGGATCACCT CTGTTCTGAC CATGACCACG 1020 TTGGGCACCTTTTCTCGTAA GAATTTCCCG CGTGTCTCCT ATATCACAGC CTTGGATTTC 1080 TATATCGCCATCTGCTTCGT CTTCTGCTTC TGCGCTCTGT TGGAGTTTGC TGTGCTCAAC 1140 TTCCTGATCTACAACCAGAC AAAAGCCCAT GCTTCTCCTA AACTCCGCCA TCCTCGTATC 1200 GATAGCCGTGCCCATGCCCG TACCCGTGCA CGTTCCCGAG CCTGTGCCCG CCAACATCAG 1260 GAAGCTTTTCTGTGCCAGAT TGTCACCACT GAGGGAAGTG ATGGAGAGGA GCGCCCGTCT 1320 TGCTCAGCCCAGCAGCCCCC TACCCCAGGT AGCCCTGAGG GTCCCCGCAG CCTCTGCTCC 1380 AAGCTGGCCTGCTGTGAGTG GTGCAAGCGT TTTAAGAAGT ACTTCTGCAT GGTCCCCGAT 1440 TGTGAGGGCAGTACCTGGCA GCAGGGCCGC CTCTGCATCC ATGTCTACCG CCTGGATAAC 1500 TACTCGAGAGTTGTTTTCCC AGTGACTTTC TTCTTCTTCA ATGTGCTCTA CTGGCTTGTT 1560 TGCCTTAACTTGTAGGTACC AGCTGGTACC CTGTGGGGCA ACCTCTCCAG TTCCCCAGGA 1620 GGTCCAAGCCCCTTGCCAAG GGAGTTGGGG GAAAGCAGCA GCAGCAGCAG GAGCGACTAG 1680 AGTTTTTCCTGCCCCATTCC CCAAACAGAA GCTTGCAGAG GGTTTGTCTT TGCTGCCCCT 1740 CTCCCCTACCTGGCCCATTC ACTGAGTCTT CTCAGCAGAC CATTTCAAAT TATTAATAAA 1800 TGGGCCACCTCCCTCTTCTT CAAGGAGCAT CCGTGATGCT CAGTGTTCAA AACCACACCC 1860 ACTTAGTGATCACCTCCCTA AAACCATGCC TAAGTACACC CGJATTAGCT ATCTTCCAAC 1920 AATGCTGACCACCAGACAAT TACTGCATTT TTCCAGAACC CCACTATTGC CTTTGTAGTG 1980 CTTTCGGCCCAGTTCTGGCC TCACCCTCAA AGTGCACCGA CTAGTTGCTT GCCTATACCT 2040 GGCACCTCATTAAGATGCTG GGCAGCAGTA TAACAGGAGG AAGAGATCCC TCTCCTTTGG 2100 TCAGATTATTATCTTCTCAG TTCTCTCTCC CTGCTACCCC TTTCTCTGCA GATAGATAGA 2160 CACTGGCATTATCCCTTTAG GAAGAGGGGG GGGCAGCAAG AGAGCCTATT TGGGACAGCA 2220 TTCCTCTCTCTCTGCTGCTG TGACATCTCC CTCTCCTTGC TGGCTCCATC TTTCGTCTGC 2280 ACTACCAATTCAATGCCCTT CATCCAATGG GTATCTATTT TTGTGTGTGA TTATAGTAAC 2340 TACTCCCTGCTTTATATGCC ACCCTCTTCC TTCTCTTTGA CCCCTGTGAC TCTTTCTGTA 2400 ACTTTCCCAGTGACTTCCCC TAGCCCTGAC CCAGGCACTA GGCCTTGGTG ACTTCCTGGG 2460 GCCAAGAAACTAAGGAAACT CGGCTTTGCA ACAGGCATTA CTCGCCATTG ATTGGTGCCC 2520 ACCCAGGGCACACTGTCGGA GTTCTATCAC TTGCTTGACC CCTGGACCCA TAAACCAGTC 2580 CACTGTTATACCCGGGGCAC TCTAACCATC ACAATCAATC AATCAAATTC CCTTAAATTT 2640 GTATGGCACTGGAACTTTGG CAAAGCACTT TTGACAAGTT GTGTCTGATT GGAGCTTCAT 2700 GATAGCCTTGTGACATCTTT AGGGGAGGAT TCTTATCCCC ATTTTGCAGA TGAAAACCCT 2760 GAGTCACAGATTTCTGTGGG ACTGTGGATC TCACTGGAAG CTATCCAAGA GCCCACTGTC 2820 ACCTTCTAGACCACATGATA GGGCTAGACA GCTCAGTTCA CCATGATTCT CTTCTGTCAC 2880 CTCTGCTGGCACACCAGTGG CAAGGCCCAG AATGGCGACC TCTCTTTAGC TCAATTTCTG 2940 GGCCTGAGGTGCTCAGACTG CCCCCAAGAT CAAATCTCTC CTGGCTGTAG TAACCCAGTG 3000 GAATGAATTTGGACATGCCC CAATGCTTCT ATATGCTAAG TGAAATCTGT GTCTGTAATT 3060 TGTTGGGGGGTGGATAGGGT GGGGTCTCCA TCTACTTTTT GTCACCATCA TCTGAAATGG 3120 GGAAATATGTAAATAAATAT ATCAGCAAAG CAAAAAGAAA AAAAAAAA Seq ID NO 4 Protein sequenceProtein Accession #: NP_004952.11          11         21         31         41         51|          |          |          |          |          | MLSKVLPVLLGILLILQSRV EGPQTESKNE ASSRDVVYGP QPQPLENQLL SEETKSTETE 60 TGSRVGKLPEASRILNTILS NYDNKLRPGI GEKPTVVTVE IAVNSLGPLS ILDMEYTIDI 120 IFSQTWYDERLCYNDTFESL VLNGNVVSQL WIPDTFPRNS KRTNENEITN PNQMVRIYKD 180 GKVLYTIRMTIDAGCSLHML RPPMDSNSCP LSPSSPSYPE NENIYKMENF KLEINEKNSW 240 KLFQFDFTGVSNKTEIITTP VGDFMVMTIF PNVSRRFGYV APDNYVPSSV TTMLSWVSFW 300 IKTESAPARTSLGITSVLTM TTLGTFSRKN PPRVSYITAL DFYIAICFVF CFCALLEFAV 360 LNFLIYNQTKANASPKLRHP RINSRAHART RARSRACARQ HQEAPVCQIV TTEGSDGEER 420 PSCSAQQPPSPGSPEGPRSL CSKLACCEMC KRFKKYPCMV PDCEGSTWQQ GRLCINVYRL 480 DNYSRVVFPVTFFFFNVLYW LVCLNL Seq ID NO 5 DNA sequence Nucleic Acid Accession #:NM_021984.1 Coding Sequence: 572..17531          11         21         31         41         51|          |          |          |          |          | GCCAGAGCGTGAGCCGCGAC CTCCGCGCAG GTGGTCGCGC CGGTCTCCGC GGAAATGTTG 60 TCCAAAGTTCTTCCAGTCCT CCTAGGCATC TTATTGATCC TCCAGTCGAG AACATGTATA 120 CAGAGAAGTGCTCAAATCAT AAGTGTACAG CTGATGAGTT GTCAAAAAAT GACCACAGCG 180 GTGTAAAGAAAGCCAAATCA AGGACCCGAA TGTGAGCAGG ACCGCAGAAG CCCCCTTTGT 240 CACTGCCTCCCAGCAAAGGC AGCACTATCC GGACTTCTAA CACCATCGGG TCGAGGGACC 300 TCAGACTGAATCAAAGAATG AAGCCTCTTC CCGTGATGTT GTCTATGGCC CCCAGCCCCA 360 GCCTCTGGAAAATCAGCTCC TCTCTGAGGA AACAAAGTCA ACTGAGACTG AGACTGGGAG 420 CAGAGTTGGCAAACTGCCAG AAGCCTCTCG CATCCTGAAC ACTATCCTGA GTAATTATGA 480 CCACAAACTGCGCCCTGGCA TTGGAGAGAA GCCCACTGTG GTCACTGTTG AGATCTCCGT 540 CAACAGCCTTGGTCCTCTCT CTATCCTAGA CATGGAATAC ACCATTGACA TCATCTTCTC 600 CCAGACCTGGTACGACGAAC GCCTCTGTTA CAACGACACC TTTGAGTCTC TTGTTCTGAA 660 TGGCAATGTGGTGAGCCAGC TATGGATCCC GGACACCTTT TTTAGGAATT CTAAGAGGAC 720 CCACGAGCATGAGATCACCA TGCCCAACCA GATGGTCCGC ATCTACAAGG ATGGCAAGGT 780 GTTGTACACAATTAGGATGA CCATTGATGC CGGATGCTCA CTCCACATGC TCAGATTTCC 840 AATGGATTCTCACTCTTGCC CTCTATCTTT CTCTAGCTTT TCCTATCCTG AGAATGAGAT 900 GATCTACAAGTGGGAAAATT TCAAGCTTGA AATCAATGAG AAGAACTCCT GGAAGCTCTT 960 CCAGTTGGATTTTACAGGAG TGAGCAACAA AACTGAAATA ATCACAACCC CAGTTGGTGA 1020 CTTCATGGTCATGACGATTr TCTTCAATGT GAGCAGGCGG TTTGGCTATG TTGCCTTTCA 1080 AAACTATGTCCCTTCTTCCG TGACCACGAT GCTCTCCTGG GTTTCCTTTT GGATCAAGAC 1140 AGAGTCTGCTCCAGCCCGGA CCTCTCTAGG GATCACCTCT GTTCTGACCA TGACCACGTT 1200 GGGCACCTTTTCTCGTAAGA ATTTCCCGCG TGTCTCCTAT ATCACAGCCT TGGATTTCTA 1260 TATCGCCATCTGCTTCGTCT TCTGCTTCTG CGCTCTGTTG GAGTTTGCTG TGCTCAACTT 1320 CCTGATCTACAACCAGACAA AAGCCCATGC TTCTCCTAAA CTCCGCCATC CTCGTATCAA 1380 TAGCCGTGCCCATGCCCGTA CCCGTGCACG TTCCCGAGCC TGTGCCCGCC AACATCAGGA 1440 AGCTTTTGTGTGCCAGATTG TCACCACTGA GGGAAGTGAT GGAGAGGAGC GCCCGTCTTG 1500 CTCAGCCCAGCAGCCCCCTA GCCCAGGTAG CCCTGAGGGT CCCCGCAGCC TCTGCTCCAA 1580 GCTGGCCTGCTGTGAGTGGT GCAAGCGTTT TAAGAAGTAC TTCTGCATGG TCCCCGATTG 1620 TGAGGGCAGTACCTGGCAGC AGGCCCGCCT CTGCATCCAT GTCTACCGCC TGGATAACTA 1680 GTCGAGAGTTGTTTTCCCAG TGACTTTCTT CTTCTTCAAT GTGCTCTACT GGCTTGTTTG 1740 CCTTAACTTGTAGGTACCAG CTGGTACCCT GTGGGGCAAC CTCICCAGTT CCCCAGGAGG 1800 TCCAAGCCCCTTCCCAAGGG AGTTGGGGGA AAGCAGCAAC AGCAGCAGGA GCGACTAGAG 1860 TTTTTCCTGCCCCATTCCCC AAACAGAAGC TTGCAGAGGG TTTGTCTTTG CTCCCCCTCT 1920 CCCCTACCTGGCCCATTCAC TGAGTTTTCT CASCAGACCA TTTCAAATTA TTAATAAATG 1980 GGCCACCTCCCTCTTCTTCA AGGAGCATCC GTGATCCTCA GTGTTCAAAA CCACAGCCAC 2040 TTAGTGATCAGCTCCCTAAA ACCATGCCTA AGTACAGGCC CATTAGCTAT CTTCCAACAA 2100 TGCTCACCACCAGACAATTA CTGCATTTTT CCAGAAGCCC ACTATTCCCT TTGCAGTGCT 2160 TTCGGCCCAGTTCTCGCCTC AGCCTCAAAD TCCACCGACT AGTTGCTTGC CTATACCTGG 2220 CACCTCATTAACATGCTGGG CAGCAGTATA ACAGGAGGAA CAGATCCCTC TCCTTTGGTC 2280 AGATTATTATGTTCTCAGTT CTCTCTCCCT GCTACCCCTT TCTCTGCAGA TAGATAGACA 2340 CTGGCATTATCCCTTTAGGA AGAGGGGGGG GCAGCAAGAG ACCCTATTTG GGACAGCATT 2400 CCTCTCTCTCTGCTGCTGTG ACATCTCCCT CTCCTTGCTG GCTCCATCTT TCGTCTGCAC 2460 TACCAATTCAATGCCCTTCA TCCAATGGGT ATCTATTTTT GTGTGTGATT ATAGTAACTA 2520 CTCCCTGCTTTATATGCCAC CCTCTTCCTT CTCTTTGACC CCTGTGACTC TTTCTGTAAC 2580 TTTCCCAGTGACTTCCCCTA GCCCTGACCC AGGCACTAGG CCTTGGTGAC TTCCTGGGGC 2640 CAAGAAACTAAGGAAACTCG GCTTTGCAAC AGGCATTACT CGCCATTGAT TGGTGCCCAC 2700 CCAGGGCACACTGTCGGAGT TCTATCACTT GCTTGACCCC TGGACCCATA AACCAGTCCA 2760 CTGTTATACCCGGGGCACTC TAACCATCAC AATCAATCAA TCAAATTCCC TTAAATTTGT 2820 ATGGCACTGGAACTTTGGCA AAGCACTTTT GACAAGTTGT GTCTGATTGG AGCTTCATGA 2880 TAGCCTTGTGACATCTTTAG GGCAGGATTC TTATCCCCAT TTTGCAGATG AAAACCCTGA 2940 GTCACAGATTTCTGTGGGAC TGTGGATCTC ACTGGAAGCT ATCCAAGAGC CCACTGTCAC 3000 CTTCTAGACCACATGATAGG GCTAGACAGC TCAGTTCACC ATGATTCTCT TCTGTCACCT 3060 CTGCTGGCACACCAGTGGCA AGGCCCAGAA TGGCGACCTC TCTTTAGCTC AATTTCTGGG 3120 CCTGAGGTGCTCAGACTGCC CCCAAGATCA AATCTCTCCT GGCTGTAGTA ACCCAGTGGA 3180 ATGAATTTGGACATGCCCCA ATGCTTCTAT ATGCTAAGTG AAATCTGTGT CTGTAATTTG 3240 TTGGGGGGTGGATAGGGTGG GGTCTCCATC TACTTTTTGT CACCATCATC TGAAATGGGG 3300 AAATATGTAAATAAATATAT CAGCAAAGC Seq ID NO 6 Protein sequence Protein Accession #:NP_068819.1 1          11         21         31         41         51|          |          |          |          |          | MEYTIDIIPSQTWYDERLCY NDTFESLVLN GNVVSQLWIP DTFFRNSKRT HENEITNPNQ 60 MVRIYKDGKVLYTIRNTIDA GCSLNNLRFP MDSNSCPLSP SSPSYPENEM IYKWENFKLE 120 INEKNSWKLFQLDFTGVSNK TEIITTPVGD FNVMTIFFNV SRRFGYVAFQ NYVPSSVTTM 180 LSWVSFWIKTESAPARTSLG ITSVLTMTTL GTPSRNMPPR VSYITALDFY IAICPVFCFC 240 ALLEPAVLNFLIYNQTKANA SPKLPNPRIN SRAHARTRAR SRACARQHQE AFVCQIVTTE 300 GSDGEERPSCSAQQPPSPGS PEGPESLCSK LACCEWCKRF KKYPCMVPDC EGSTWQQARL 360 CINVYRLDNYSRVVFPVTFP FPNVLYWLVC LNL Seq ID NO 7 DNA sequence Nucleic AcidAccession #: NM_021987.1 Coding sequence 672..16571          11         21         31         41         51|          |          |          |          |          | GCCAGAGCGTGAGCCGCGAC CTCCGCGCAG GTGGTCGCGC CGGTCTCCGC GGAAATGTTG 60 TCCAAAGTTCTTCCAGTCCT CCTAGGCATC TTATTGATCC TCCAGTCGAG AACATGTATA 120 CAGAGAAGTGCTCAAATCAT AAGTGTACAG CTGATGAGTT GTCAAAAAAT GACCACAGCG 180 GTGTAAAGAAAGGCAAATCA AGGACCCGAA TGTGAGCAGG ACCTCAGAAG CCCCCTTTGT 240 CACTGCCTCCCAGCAAAGGC AGCACTATCC GGACTTCTAA CACCATCGGG TCGAGGGACC 300 TCAGACTGAATCAAAGAATG AAGCCTCTTC CCGTGATGTT GTCTATGGCC CCCAGCCCCA 360 GCCTCTGGAAAATCAGCTCC TCTCTGAGGA AACAAAGTCA ACTGAGACTG AGACTGGGAG 420 CAGAGTTGGCAAACTGCCAG AAGCCTCTCG CATCCTGAAC ACTATCCTGA GTAATTATGA 480 CCACAAACTGCGCCCTGGCA TTGGAGAGAA GCCCACTGTG GTCACTGTTG AGATCTCCGT 540 CAACAGCCTTGGTCCTCTCT CTATCCTAGA CATGGAATAC ACCATTGACA TCATCTTCTC 600 CCAGACCTGGAATTCTAAGA GGACCCACGA GCATGAGATC ACCATGCCCA ACCAGATGGT 660 CCGCATCTACAAGGATGGCA AGGTGTTGTA CACAATTAGG ATGACCATTG ATGCCGGATG 720 CICACTCCACATGCTCAGAT TTCCAATGGA TTCTCACTCT TGCCCTCTAT CTTTCTCTAG 780 CTTTTCCTATCCTGAGAATG AGATGATCTA CAAGTGGGAA AATTTCAAGC TTGAAATCAA 840 TGAGAAGAACTCCTGGAAGC TCTTCCAGTT TGATITTACA GGAGTGAGCA ACAAAACTGA 900 AATAATCACAACCCCAGTTG GTGACTTCAT GGTCATGACG ATTTTCTTCA ATGTGAGCAG 960 GCGGTTTGGCTATGTTGCCT TTCAAAACTA TGTCCCTTCT TCCGTGACCA CGATGCTCTC 1020 CTGGGTTTCCTTTTGGATCA AGACAGAGTC TGCTCCAGGC CGGACCTCTC TAGGGATCAC 1080 CTCTGTTCTGACCATGACCA CGTTGGGCAC CTTTTCTCGT AAGAATTTCC CGCGTGTCTC 1140 CTATATCACAGCCTTGGATT TCTATATCGC CATCTGCTTC GTCTTCTGCT TCTGCGCTCT 1200 GTTGGAGTTTGCTGTGGTCA ACTTCCTGAT CTACAACCAG ACAAAAGCCC ATGCTTCTCC 1260 TAAACTCCGCCATCCTCGTA TCAATAGCCG TGCCCATGCC CGTACCCGTG CACGTTCCCG 1320 AGCCTGTGCCCGCCAACATC AGGAAGCTTT TGTGTDCCAG ATTGTCACCA CTGAGGGAAG 1380 TGATGGAGAGGAGCGCCCGT CTTGCTCAGC CCAGCAGCCC CCTAGCCCAG GTAGCCCTGA 1440 GGGTCCCCGCAGCCTCTGCT CCAAGCTGGC CTGCTGTGAG TGGTGCAAGC GTTTTAAGAA 1500 GTACTTCTGCATGGTCCCCG ATTGTGAGGG CAGTACCTGG CAGCAGGGCC GCCTCTGCAT 1560 CCATGTCTACCGCCTGGATA ACTACTCGAG AGTTGTTTTC CCAGTGACTT TCTTCTTCTT 1620 CAATGTGCTCTACTGGCTTG TTTGCCTTAA CTTGTAGGTA CCAGCTGGTA CCCTGTGGGG 1680 CAACCTCTCCAGTTCCCCAG GAGGTCCAAG CCCCTTGCCA AGGGAGTTGG GGGAAAGCAG 1740 CAGCAGCAGCAGGAGGGACT AGAGTTTTTC CTGCCCCATT CCCCAAACAG AAGCTTGCAG 1800 AGGGTTTGTCTTTGCTGCCC CTCTCCCCTA CCTGGCCCAT TCACTGAGTT TTCTCAGCAG 1860 ACCATTTCAAATTATTAATA AATGGGCCAC CTCCCTCTTC TTCAAGGAGC ATCCGTGATG 1920 CTCAGTGTTCAAAACCACAG CCACTTAGTG ATCAGCTCCC TAAAACCATG CCTAAGTACA 1980 GGCGGATTAGCTATCTTCCA ACAATGCTGA CCACCAGACA ATTACTGCAT TTTTCCAGAA 2040 GCCCACTATTGCCTTTGCAG TGCTTTCGGC CCAGTTCTGG CCTGAGCCTC AAAGTGCACC 2100 GACTAGTTGCTTGCCTATAC CTGGCACCTC ATTAAGATGC TCGGCAGCAG TATAACAGGA 2160 GGAAGAGATCCCTCTCCTTT GGTCAGATTA TTATGTTCTC AGTTCTCTCT CCCTGCTACC 2220 CCTTTCTCTGCAGATAGATA GACACTGGCA TTATCCCTTT AGGAAGACGG GGGGGCAGCA 2280 AGAGAGCCTATTTGGGACAG CATTCCTCTC TCTCTGCTGC TGTGACATCT CCCTCTCCTT 2340 GCTGGCTCCATCTTTCGTCT GCACTACCAA TTCAATGCCC TTCATCCAAT GGGTATCTAT 2400 TTTTGTGTGTGATTATAGTA ACTACTCCCT GCTTTATATG CCACCCTCTT CCTTCTCTTT 2460 GACCCCTGTGACTCTTTCTG TAACTTTCCC AGTGACTTCC CCTAGCCCTG ACCAGGCACT 2520 AGGCCTTGGTGACTTCCTGG GGCCAACAAA CTAAGGAAAC TCGGCTTTGC AACAGGCATT 2580 ACTCGCCATTGATTGGTGCC CACCGAGGGC ACACTGTCGG AGTTCTATCA CTTGCTTGAC 2640 CCCTGGACCCATAAACCAGT GCACTGTTAT ACCCGGGGCA CTCTAACCAT CACAATCAAT 2700 CAATCAAATTCCCTTAAATT TGTATGGCAC TGGAACTTTG GCAAAGCACT TTTGACAAGT 2760 TGTGTCTGATTGGAGCTTCA TGATAGCCTT GTGACATCTT TAGGGCAGGA TTCTTATCCC 2820 CATTTTGCAGATGAAAACCC TGAGTCACAG ATTTCTGTGG GACTGTGGAT CTCACTGGAA 2880 GCTATCCAAGAGCCCACTGT CACCTTCTAG ACCACATGAT AGGGCTAGAC AGCTCAGTTC 2940 ACCATGATTCTCTTCTGTCA CCTCTGCTGG CACACCACTG GCAAGGCCCA GAATGGCGAC 3000 CTCTCTTTAGCTCAATTTCT GGGCCTGAGG TGCTCAGACT GCCCCCAAGA TCAAATCTCT 3060 CCTGGCTGTAGTAACCCAGT GGAATGAATT TGGACATGCC CCAATGCTTC TATATGCTAA 3120 GTGAAATCTGTGTCTGTAAT TTGTTGGGGG GTGGATAGGG TGGGGTCTCC ATCTACTTTT 3180 TGTCACCATCATCTGAAATG GGGAAATATG TAAATAAATA TATCAGCAAA GC Seq ID NO: 8 Proteinsequence Protein Accession #: NP_068822.11          11         21         31         41         51|          |          |          |          |          | MEYTIDIIFSQTWNSKRTHE HEITNPNQMV RIYKDGKVLY TIRMTIDAGC SLHMLRFPMD 60 SHSCPLSFSSFSYPENNMIY KWENFKLEIN EKNSWKLFQF DFTGVSNKTE IITTPVGDFM 120 VMTIFFNVSRRFGYVAFQNY VPSSVTTMLS WVSFWIKTES APARTGLGIT SVLTMTTLGT 180 FSRKNFPRVSYITALDFYIA ICFVFCFCAL LEPAVLNFLI YNQTKAHASP KLRHPRINSN 240 AHARTPARSNACARQHQEAF VCQIVTTEGS DGEERPSCSA QQPPSPGSPE GPRSLCSKLA 300 CCEWCKRFKKYFCMVPDCEG STWQQGRLCI HVYRLDNYSR VVFPVTFFFF NVLYWLVCLN 360 L Seq ID NO:9 DNA sequence Nucleic Acid Accession #: NM_021990.1 Coding sequence:1309..2490 1          11         21         31         41         51|          |          |          |          |          | GCCAGAGGGTGAGCCGCGAC CTCCGCGCAG GTGGTCGCGC CGGTCTCCGC GGAAATGTTG 60 TCCAAAGTTCTTCCAGTCCT CCTAGGCATC TTATTGATCC TCCAGTCGAG AACATGTATA 120 CAGAGAAGTGCTCAAATCAT AAGTGTACAG CTGATGAGTT GTCAAAAAAT GACCACAGCG 180 GTGTAAAGAAAGCCAAATCA AGGACCCGAA TGTGAGCAGG ACCTCAGAAG CCCCCTTTGT 240 CACTGCCTCCCAGCAAAGGC AGCACTATCC GGACTTCTAA CACCATCGGT GAGTTTCATA 300 CCTTGGCAGATGGCCTTTAA CATTTTTGTT TAATTCAATT ATTCTTACTA ATCTTCTTCT 360 TTTTCTTGGCTGTGGTGCAT GGCTGTGGAG CTCAGGGTGG ACTCCTGTTG GGCAGCCAGT 420 TCCTGGATGGCTGTCTGTGG GTGGAGGACT CCTGCCTTTC CTGTTTAGAC ACCCACAAAG 480 GCTGCTCTTTAGCCTCCTTC CCTTCATCCC CTTCCCCtGC CCCCAGTGCA ACGAGTATTA 540 CACAACCAACAAAACCGCAA AATATTCCCA CAATTTTGTG GTCCTCTCTG GGAGAGGCCG 600 CTCTGGCTTTTCCTCTCAGC CCTGGCCCTC TGCCTGCTCC TCACTCCTGG TTGGTGCTGG 660 TCAGGCTGACTAGAGGCCAA GGCGACCAAC ACTAGGCAAA CGCGGCCAGC GCTCAGACAT 720 AAATGCCCTCTTCATTTCAC GTGTAACATT CTTTTAAAAT GTAGGTCTTG GTTTTGTTGA 780 TTTTTTCTTAAATAAAAGAG TGATCATAAA AGAGGGACAG CATAGAAAGT CCCCAAAGAG 840 CAGCAAGGTTTTAAAGAAAT TCACAAGCCT AATCTGTGAC TGTCTTATAA TTTGCTATTA 900 CCAGTCACAATTTAACTAGG TTTTGTGTTG AAAACTTGTT TTGGTTTGCT TCTGTCCCAA 960 GAGGCACTAGCTGGGGCCCC TACAGAGTGC AGGGCAGAGC TTCATTTTTC GTTTGAATGT 1020 TCTAGGGTCGAGGGACCTCA GACTGAATCA AAGAATGAAG CCTCTTCCCG TGATGTTGTC 1080 TATGGCCCCCAGCCCCAGCC TCTGGAAAAT CAGCTCCTCT CTGAGGAAAC AAAGTCAACT 1140 GAGACTGAGACTGGGAGCAG AGTTGGCAAA CTGCCAGAAG CCTCTCGCAT CCTGAACACT 1200 ATCCTGAGTAATTATGACCA CAAACTGCGC CCTGGCATTG GAGAGAAGCC CACTGTGGTC 1260 ACTGTTGAGATCTCCGTCAA CAGCCTTGGT CCTCTCTCTA TCCTAGACAT GGAATACACC 1320 ATTGACATCATCTTCTCCCA GACCTGGTAC GACGAACGCC TCTGTTACAA CGACACCTTT 1380 GAGTCTCTTGTTCTGAATGG CAATGTGGTG AGCCAGCTAT GGATCCCGGA CACCTTTTTT 1440 AGGAATTCTAAGAGGACCCA CGAGCATGAG ATCACCATGC CCAACCAGAT GGTCCGCATC 1000 TACAAGGATGGCAAGGTGTT GTACACAATT AGGATGACCA TTGATGCCGG ATGCTCACTC 1560 CACATGCTCAGATTTCCAAT GGATTCTCAC TCTTGCCCTC TATCTTTCTC TAGCTTTTCC 1620 TATCCTGAGAATGAGATGAT CTACAAGTGG GAAAATTTCA AGCTTGAAAT CAATGAGAAG 1680 AACTCCTGGAAGCTCITCCA GTTTGATTTT ACAGGAGTGA GCAACAAAAC TGAAATAATC 1740 ACAACCCCAGTTGGTGACTT CATGGTCATG ACGATTTTCT TCAATGTGAG CAGGCGGTTT 1800 GGCTATGTTGCCTTTCAAAA CTATGTCCCT TCTTCCGTGA CCACGATGCT CTCCTGGGTT 1860 TCCTTTTGGATCAAGACAGA GTCTGCTCCA GCCCGGACCT CTCTAGGGAT CACCTCTGTT 1920 CTGACCATGACCACGTTGGG CACCTTTTCT CGTAAGAATT TCCCGCGTGT CTCCTATATC 1980 ACAGCCTTGGATTTCTATAT CGCCATCTGC TTCGTCTTCT GCTTCTGCGC TCTGTTGGAG 2040 TTTGCTGTGCTCAACTTCCT GATCTACAAC CAGACAAAAG CCCATGCTTC TCCTAAACTC 2100 CGCCATCCTCGTATCAATAG CCGTGCCCAT GCCCGTACCC GTGCACGTTC CCGAGCCTGT 2160 GCCCGCCAACATCAGGAAGC TTTTGTGTGC CAGATTGTCA CCACTGAGGG AAGTGATGGA 2220 GAGGAGCGCCCGTCTTGCTC AGCCCAGCAG CCCCCTAGCC CAGGTAGCCC TGAGGGTCCC 2280 CGCAGCCTCTGCTCCAAGCT GGCCTGCTGT GAGTGGTGCA AGCGTTTTAA GAAGTACTTC 2340 TGCATGGTCCCCGATTGTGA GGGCAGTACC TGGCAGCAGG GCCGCCTCTG CATCCATGTC 2400 TACCGCCTGGATAACTACTC GAGAGTTGTT TTCCCAGTGA CTTTCTTCTT CTTCAATGTG 2460 CTCTACTGGCTTGTTTGCCT TAACTTGTAG GTACCAGCTG GTACCCTGTG GGGCAACCTC 2520 TCCAGTTCCCCAGGAGGTCC AAGCCCCTTG CCAAGGGAGT TGGGGGAAAG CAGCAGCAGC 2580 AGCAGGAGCGACTAGAGTTT TTCCTGCCCC ATTCCCCAAA CAGAAGCTTG CAGAGGGTTT 2640 GTCTTTGCTGCCCCTCTCCC CTACCTGGCC CATTCACTCA GTTTTCTCAG CAGACCATTT 2700 CAAATTATTAATAAATGGGC CACCTCCCTC TTCTTCAAGG AGCATCCGTG ATGCTCAGTC 2760 TTCAAAACCACAGCCACTTA GTGATCAGCT CCCTAAAACC ATGCCTAAGT ACAGGCGGAT 2820 TAGCTATCTTCCAACAATGC TGACCACCAG ACAATTACTG CATTTTTCCA GAAGCCCACT 2880 ATTGCCTTTGCAGTGCTTTC GGCCCAGTTC TGGCCTCAGC CTCAAAGTGC ACCCACTAGT 2940 TGCTTGCCTATACCTGGCAC CTCAATAAGA TGCTGGGCAG CAGTATAACA CCAGGAAGAG 3000 ATCCCTCTCCTTTGGTCAGA TTATTATGTT CTCAGTTCTC TCTCCCTGCT ACCCCTTTCT 3060 CTGCAGATAGATAGACACTG GCATTATCCC TTTAGGAAGA GGGGGGGGCA GCAAGAGAGC 3120 CTATTTGGGACAGCATTCCT CTCTCTCTGC TGCTGTGACA TCTCCCTCTC CTTGCTGGCT 3180 CCATCTTTCGTCTGCACTAC CAATTCAATG CCCTTCATCC AATGGGTATC TATTTTTGTG 3240 TGTGATTATAGTAACTACTC CCTGCTTTAT ATGCCACCCT CTTCCTTCTC TTTCACCCCT 3300 GTGACTCTTTCTGTAACTTT CCCAGTGACT TCCCCTAGCC CTGACCAGGC ACTAGGCCTT 3360 GGTGACTTCCTGGGGCCAAG AAACTAAGGA AACTCGGCTT TGCAACAGGC ATTACTCGCC 3420 ATTGATTGGTGCCCACCCAG CCCACACTGT CGGAGTTCTA TCACTTGCTT GACCCCTGGA 3480 CCCATAAACCAGTCCACTGT TATACCCGGG GCACTCTAAC CATCACAATC AATCAATCAA 3540 ATTCCCTTAAATTTGTATGG CACTGGAACT TTGGCAAAGC ACTTTTGACA AGTTGTGTCT 3600 CATTGGAGCTTCATGATAGC CTTGTGACAT CTTTAGGGCA GGATTCTTAT CCCCATTTTG 3660 CAGATGAAAACCCTGAGTCA CAGATTTCTG TGGGACTGTG GATCTCACTG GAAGCTATCC 3720 AAGAGCCCACTGTCACCTTC TAGACCACAT GATAGGGCTA GACAGCTCAG TTCACCATGA 3780 TTCTCTTCTGTCACCTCTGC TGGCACACCA GTGGCAAGGC CCAGAATGGC GACCTCTCTT 3840 TAGCTCAATTTCTGGGCCTG AGGTGCTCAG AGTGCCCCGA AGATCAAATC TCTCCTGGCT 3900 GTAGTAACCCAGTGGAATGA ATTTGGACAT GCCCCAATGC TTCTATATGC TAAGTGAAAT 3960 CTGTGTCTGTAATTTGTTGG GGGGTGGATA GGGTGGGGTC TCCATCTACT TTTTGTCACC 4020 ATCATCTGAAATGGGGAAAT ATGTAAATAA ATATATCAGC AAAGC Seq ID NO: 10 Protein sequenceProtein Accession #: NP_068830.11          11         21         31         41         51|          |          |          |          |          | MEYTIDIIPSQTWYDERLCY NDTFESLVLN GNVVSQLWIP DTFFRNSKRT HENEITNPNQ 60 MVRIYKIGKVLYTIRMTIDA GCSLHNLRFP MDSNSCPLSF SSFSYPENEM IYKWENFKLE 120 INEKNSWKLFQFDFTGVSNK TEIITTPVGD FMVMTIFFNV SRRFGYVAFQ NYVPSSVTTM 180 LSWVSFWIKTESAPARTSLG ITSVLTMTTL GTFSRKNFPR VSYITALDFY IAICFVFCFC 240 ALLEFAVLNFLIYNQTKANA SPKLRNPRIN SPAHARTEAR SRACARQNQE AFVCQIVTTE 300 GSDGEERPSCSAQOPPSPGS PEGPRSLCSK LACCEWCKRF KKYFCMVPDC EGSTWQQGRL 360 CINVYRLDNYSRVVFPVTPF FFNVLYWLVC LNL Seq ID NO: 11 DNA sequence Nucleic AcidAccession #: NM_001076.1 Coding sequence: 22..16141          11         21         31         41         51|          |          |          |          |          | TTCGGCACGAGTAAGACCAG GATGTCTCTG AAATGGACGT CAGTCTTTCT GCTGATACAG 60 CTCAGTTGTTACTTTAGCTC TGGAAGCTGT GGAAAGGTGC TAGTGTGGCC CACACAATAC 120 AGCCATTGOATAAATATGAA GACAATCCTG GAAGAGCTTG TTCAGAGGGG TCATGAGGTG 180 ACTGTGTTGACATCTTCGGC TTCTACTCTT GTCAATGCCA GTAAATCATC TGCTATTAAA 240 TTAGAAGTTTATCCTACATC TTTAACTAAA AATGATTTGG AAGATTCTCT TCTGAAAATT 300 CTCGATAGATGGATATATGG TGTTTCAAAA AATACATTTT GGTCATATTT TTCACAATTA 360 CAAGAATTGTGTTGGGAATA TTATGACTAC AGTAACAAGC TCTGTAAAHA TGCAGTTTTG 420 AATAAGAAACTTATGATGAA ACTACAAGAG TCAAAGTTTG ATGTCATTCT GGCAGATGCC 480 CTTAATCCCTGTGGTGAGCT ACTGGCTGAA CTATTTAACA TACCCTTTCT GTACAGTCTT 540 CGATTCTCTGTTGGCTACAC ATTTGAGAAG AATGGTGGAG GATTTCTGTT CCCTCCTTCC 600 TATGTACCTGTTGTTATGTC AGAATTAAGT GATCAAATGA TTTTCATGGA GAGGATAAAA 660 AATATGATACATATGCTTTA TTTTGACTTT TGGTTTCAAA TTTATGATCT GAAGAAGTGG 720 GACCAGTTTTATAGTGAAGT TCTAGGAAGA CCCACTACAT TATTTGAGAC AATGGGGAAA 780 GCTGAAATGTGGCTCATTCG AACCTATTGG GATTTTGAAT TTCCTCGCCC ATTCTTACCA 840 AATGTTGATTTTGTTGGAGG ACTTCACTGT AAACCAGCCA AACCCCTGCC TAAGGAAATG 900 GAAGAGTTTGTGCAGAGCTC TGGAGAAAAT GGTATTGTGG TGTTTTCTCT GGGGTCGATG 960 ATCAGTAACATGTCAGAAGA AAGTGCCAAC ATGATTGCAT CAGCCCTTGC CCAGATCCCA 1020 CAAAAGGTTCTATGGAGATT TGATGGGAAG AAGCCAAATA CATTAGGTTC CAATACTCGA 1080 CTGTACAAGTGGTTACCCCA GAATGACCTT CTTGGTCATC CCAAAACCAA AGCTTTTATA 1140 ACTCATGGTGGAACCAATGG CATCTATGAG GCGATCTACC ATGGGATCCC TATGGTGGTC 1200 ATTCCCTTGTTTGCGGATCA ACATGATAAC ATTGCTCACA TGAAAGCCAA GGGAGCAGCC 1260 CTCAGTGTGGACATCAGGAC GATGTCAAGT AGAGATTTGC TCAATGCATT GAAGTCAGTC 1320 ATTAATGACCCTGTCTATAA AGAGAATGTC ATGAAATTAT CAAGAATTCA TCATGACCAA 1380 CCAATGAAGCCCCTGGATCG AGCAGTCTTC TGGATTGAGT TTGTCATGCG CCACAAAGGA 1440 GCCAAGCACCTTCGAGTCGC AGCTCACAAC CTCACCTGGA TCGAGTACCA CTCTTTGGAT 1500 GTGATAGCATTCCTGCTGGC CTGCGTGGCA ACTGTGATAT TTATCATCAC AAAATTTTGC 1560 CTGTTTTGTTTCCGAAAGCT TGCCAAAACA GGAAAGAAGA AGAAAAGAGA TTAGTTATAT 1620 CAAAAGCCTGAAGTGGAATG ACTGAAAGAT GGGACTCCTC CTTTATTTCA GCATGGAGGG 1680 TTTTAAATGGAGGATTTCCT TTTTCCTGTG ACAAAACATC TTTTCACAAC TTACCTTGTT 1740 AAGACAAAATTTATTTTCCA GGGATTTAAT ACGTACTTTA GTTGGAATTA TTCTATGTCA 1800 ATGATTTTTAAGCTATGAAA AATACAATGG GGGGAAGGAT AGCATTTGGA GATATACCTA 1860 ATGTTAAATGACGAGTTACT GGATGCAGGA CGCAACATGG CACATGTGTA TACATATGTA 1920 GCTAACCCTTCGTTGTGCAC ATGTACCCTA AAACTTAAAG TATAATTTAA AAAAAGCAAA 1980 AAAAAAAAATACCAACTCTT TTTTTTAAAC CAGGAAGGAA AATGTGAACA TGGAAACAAC 2040 TTCTAGTATTGGATCTGAAA ATAAAGTGTC ATCCAAGCCA TAAAAAAAAA Seq ID NO: 12 Proteinsequence Protein Accession #: NP_001067.11          11         21         31         41         51|          |          |          |          |          | MSLKWTSVFLLIQLSCYFSS GSCGKVLVWP TEYSHWINMK TILEELVQRG HEVTVLTSSA 60 STLVNASKSSAIKLEVYPTS LTKNDLEDGL LKILDRWIYG VSKNTFWSYF SQLQELCWEY 120 YDYSNKLCKDAVLNKKLMMK LGEGKFDVIL ADALNPCGEL LAELFNIPFL YSLRFSVGYT 180 FEKNGGGGFLPPSYVPVVNS ELSDQMIFME RIKNMINMLY FDFWFQIYDL KKWDQFYSEV 240 LGRPTTLFETMGKAEMWLIR TYWDFEFPRP FLPNVDFVGG LNCKPAKPLP KENEEFVQSS 300 GENGIVVFSLGSMISNNSEE SANMIASALA QIPQKVLWRF DGKKPNTLCS NTRLYKWLPQ 360 NDLLGNPKTKAFITNGGTNG IYSAIYNGIP MVGIPLFADQ HDNIAHMKAK GAALSVDIRT 420 NSSRDLLNALKSVINDPVYK ENVMKLSRIN NDQPMKPLDR AVFWIEFVMR HKGAKHLRVA 480 AHNLTWIQYNSLDVIAFLLA CVATVIFIIT KFCLFCPRKL AKTGKKKKRD Seq ID NO 13 DNA sequenceNucleic Acid Accession #: NN_014109 1 Coding sequence: 651..17391          11         21         31         41         51|          |          |          |          |          | CTGTCATTCATGCTTTGGAA AAGTTTACTG TATATACATT AGACATTCCT GTTCTTTTTG 60 GAGTTAGTACTACATCCCCT GAAGAAACAT GTGCCCAGGT GATTCGTGAA GCTAAGAGAA 120 CAGCACCAAGTATAGTGTAT GTTCCTCATA TCCACGTGTG GTGGGAAATA GTTGGACCGA 180 CACTTAAAGCCACATTTACC ACATTATTAC AGAATATTCC TTCATTTGCT CCAGTTTTAC 240 TACTTGCAACTTCTGACAAA CCCCATTCCG CTTTGCCAGA AGAGGTGCAA GAATTGTTTA 300 TCCGTGATTATGGAGAGATT TTTAATGTCC AGTTACCGGA TAAADAAGAA CGGACAAAAT 360 TTTTTGAAGATTTAATTCTA AAACAAGCTG CTAAGCCTCC TATATCAAAA AAGAAAGCAG 420 TTTTGCAGGCTTTGGAGGTA CTCCCAGTAG CACCACCACC TGAGCCAAGA TCACTGACAG 480 CAGAAGAAGTGAAACGACTA GAAGAACAAG AAGAAGATAC ATTTAGAGAA CTGAGGATTT 540 TCTTAAGAAATGTTACACAT AGGCTTGCTA TTGACAAGCG ATTCCGAGTG TTTACTAAGC 800 CTGTTGACCCTGATGAGGTT CCTGATTATG TCACTGTAAT AAAGCAACCA ATGGACCTTT 680 CATCTGTAATCAGTAAAATT GATCTACACA AGTATcTGAC TGTGAAAGAC TATTTGAGAG 720 ATATTGATCTAATCTGTAGT AATGCCTTAG AATACAATCC AGATAGAGAT CCTGGAGATC 780 GTCTTATTAGGCATAGAGCC TGTGCTTTAA GAGATACTGC CTATGCCATA ATTAAAGAAG 840 AACTTGATGAAGACTTTGAG CAGCTCTGTG AAGAAATTCA GGAATCTAGA AAGAAAAGAG 900 GTTGTAGCTCCTCCAAATAT GCCCCGTCTT ACTACCATGT GATGCCAAAG CAAAATTCCA 960 CTCTTGTTGGTGATAAAAGA TCAGACCCAG AGCAGAATGA AAAGCTAAAG ACACCGAGTA 1020 CTCCTGTGGCTTGCAGCACT CCTGCTCAGT TGAAGAGGAA AATTCGCAAA AAGTCAAACT 1080 GGTACTTAGGCACCATAAAA AAGCGAAGGA AGATTTCACA GGCAAAGGAT GATAGCCAGA 1140 ATGCCATAGATCACAAAATT GAGAGTGATA CAGAGGAAAC TCAAGACACA AGTGTAGATC 1200 ATAATGAGACCGGAAACACA GGAGAGTCTT CGGTGGAAGA AAATGAAAAA CAGCAAAATG 1260 CCTCTGAAAGCAAACTGGAA TTGAGAAATA ATTCAAATAC TTGTAATATA GAGAATGAGC 1320 TTGAAGACTCTAGGAAGACT ACAGCATGTA CAGAATTGAG AGACAAGATT GCTTGTAATG 1380 GAGATGCTTCTAGCTCTCAG ATAATACATA TTTCTGATGA AAATGAAGGA AAAGAAATGT 1440 GTGTTCTGCGAATGACTCGA GCTAGACGTT CCCAGGTAGA ACAGCAGCAG CTCATCACTG 1500 TTGAAAAGGCTTTGGCAATT CTTTCVCAGC CTACACCCTC ACTTGTTGTG GATCATGAGC 1560 GATTAAAAAATCTTTTGAAG ACTGTTGTTA AAAAAAGTCA AAACTACAAC ATATTTCAGT 1820 TGGAAAATTTGTATGCAGTA ATCAGCCAAT GTATTTATCG GCATCGCAAG GACCATGATA 1880 AAACATCACTTATTCAGAAA ATGGAGCAAG AGGTAGAAAA CTTCAGTTGT TCCAGATGAT 1740 GATGTCATGGTATCGAGTAT TCTTTATATT CAGTTCCTAT TTAAGTCATT TTTGTCATGT 1800 CCGCCTAATTGATGTAGTAT GAAACCCTGC ATCTTTAAGG AAAAGATTAA AATAGTAAAA 1880 TAAAAGTATTTAAACTTTCC TGATATTTAT GTACATATTA AGATAAATGT CATGTGTAAG 1920 ATAACTGATAAATA Seq ID NO: 14 Protein sequence Protein Accession #: NP_054828.11          11         21         31         41         51|          |          |          |          |          | MDLSSVISKIDLNKYLTVKD YLRDIDLICS NALEYNPDRD PGDRLIRNRA CALRDTAYAI 60 IKEELDEDEEQLCEEIQESS KKRGCSSSKY APSYYHVNPK QNSTLVGDKR SDPEQNEKLK 120 TPSTPVACSTPAQLRRKIRK KSNWTYGTIE KRRKISOAKD DSQNAIDNKI ESDTEETQDT 180 SVDHNETGNTGESSVEENEK QQNASESKLE LRNNSNTGNI ENELEDSRKT TACTELEDRI 240 ADNGDASSSQIINISDENEG KEMCVLRNTR ARRSQVEQQQ LITVEKALAI LSQPTPSLVV 300 DNERLEELLKTVVKRSQNYN IFQLENLYAV ISQCIYRNRK DHDKTSLIQK NEQEVENFSC 360 SR Seq ID NO:15 DNA sequence Nucleic Acid Accession #: AK0015381          11         21         31         41         51|          |          |          |          |          | TATATGTGACCTTTTTAAAA AATGAGCTGT AAGCAGTCTC CCAGACAGTA GCTCAGCCTC 60 CAGAACTCTCTTTCTGCATA GTTGAAGACC CCTCTTCACA CAAGATGGTA GCAACAAATC 120 ATAGGTGCAATTGCACCAAA TTCACAGAAG ATCAATTGAA AATCCTCATC AATACCTTCA 180 CTCAAAAACCTTACCCAGGT TATGCTACCA AACAAAAACT TGCTTTAGCA ATCAATGCAG 240 AAGAGTCCAGAATCCAGATT TGGTTTCAGA ATCAAAGAGC TAGGCATGGA TTCCAGAAAA 300 CACCAGAACCTGACTTTAGA TTTAAGCCAC AGCCATGGAC AAGATTAACC TGGTGTGGAG 360 TTTCAAAATAGAGAAGCCAG ATGGTGTTGT ACCACCTATA GCACCTTTCA ATTACACACA 420 ATCATCCATGCATTTATGAA AAACCCATAC CCTGGGATTG ATTCCGGAGA ACAACTTGCT 480 GAAGAAATTGGTGCTTCAGA GTCAAGAGTC CAAATTTGGT TCCAAAATCA AAGATCTAGA 540 TTTCATCTCCAGAGAAAAAG AGAACCTGTT ATGTCCTTAG AATGAGAAGA CCAGAGAAGA 600 CCAGGGGCAAGGTTTCTGAG GGACTTCAAG GTACAGAAGA TACACAAAGT GGCACCAGCC 860 TCACTAGCACTCTCATTTCT CAAGAGCCAG AACATGGTGA ATACAGTCAA GTTCAGTGTA 720 TTTGATAATATCAATTTGGG CCCCAAATCT CTCTCACAGT CTTCCTGGGA GTCTATTCTT 780 CTTCCAAAAGTGCAAGCTAA GCCTTCTGAA GATGGTAAAG AACTTGGGGA CGTGTGGTGG 840 CTCATGCCTGTAATCCCAGC ACTTTAGGAG CCTGAGGCTG CAAGATTGCT TCAGCCTAGC 900 AGTTTGAAACCAGTCTGAGC AACATAGTAA GACCCTGTCT CTATTCTAAA AAACAAAATA 900 AGTAAAAAGGACTGTAGGAG GCCAAGACAG GTACAGGAOG CACCACACTA CCCTGTTGAC 1020 ACAGCCTGGATCCAGAGTTC AGCAGACCTT CAGACAATGA AAACAAACTT AGTAATAATC 1080 ATTTTTCAATCATTGCAGTA ATTATTGATT TGGACAAAAA TCAATTGACC TCAAAACCTT 1140 AAAGTGACGTTTCTCTGCCT ATGGAGTGGT CATTCTTTTA TTCCTTTAGT TTCATAATAA 1200 ATTTTCTTTTACTTAAAAAA ACTTATAGTT TGATGAAGAG TGAGATATAT ACCTCATCTC 1260 AAAGAATCTTCACACACACA CTTATTAATT ACAAAAGGAA AATCAGTAAT TTTGCAGTGG 1320 AGACATATGGCCAACTCCAC CTTACCCAAG TGGCTGAAAG TCACTGCACC ACTAATGGCA 1380 CAAACCAATGTGAGATCATT CCTCATATDA TACACTAAAA AGGGCACTGT CTCTTCTGCA 1440 TGTTGCAGACAAAAAGTGGC TAAGCTGACA CTGAAACTAA TAATTAGGCA ATGTCAAGCA 1900 AATACAAATTCAAGTTGACA GTCTGCAAAG TAACATCCAT GTACTCTTCA ACAATGGATC 1560 CACCCTAGCTACTCAGGAGG CTGAGGTGGA ATAATTGTTT GAGGCCAGGA CTTCCAGATC 1620 AGCCTCGGCAACATCATGCG ACCCCATCTC TAAAAACATC TTTTTAAAAA TCAGCCAGGT 1680 GTGGTAGCATGCACCCGTAG TCTCAGCTAC TCAGGACCCT GAGOCAGGAG CATGGTTTCA 1740 ACATAGGAGATCGAGGCTGC TGTGAGCTAT GATCGTGCTA CTGCACTCCA GCCTGGGTGA 1800 CACAGCAAGTTCCTGTTTCC AAACAACAAC AAGAAAACAA AACAAAACAA AACAAAAAAT 1860 AGATAGAATAGTGACAATAA AAATGGAGAA AAAGTAGGCT GACTCAGGAA ATGCTTAGAA 1920 AGTACAGCCATACCTCAAAG ATATTGTAGA TTTGATTCGA GACCACCACA ATPAAGCAGA 1980 TATTGCTACAAAGTGAGTCA CACAAATTGT TTTGTTTCCT TGTGAATATG AAGTTATATT 2040 GGCTGGGTGTGATGGCTCAT GCCTATAATC CCAGTACTTT AGGAGACGGA GGCGGGAGGG 2100 TCACTTGAGCCCAGGAATTG TGAGATCAAC CTGGGCATAT AGGGAGATCC TGTCTCTATT 2160 TAAAAAAAGAAGCTATGTTT ACACTACACT ATAGTCTATT TAAAGTGTGA AATGGCGTTA 2220 TGTCCTTAATTTTAAAACTC TTGATGCTGG CTGGGTTCGG TGGCTCATAC CTGTAATCCC 2280 ATCACTTTGGGAGGCCAAGA CAGGTTGATT ACTTGAATTC AGGAGTTCAA GACCAGCCTG 2340 GACAACATGGCAAAACACGT CTTTAAAAAA AGAAAAGAAA AAAGAAAAAC AGAAAGAAAA 2400 AGAAGAAAPACTACTTGCTG CCCTTACTTG AAGCTCAATT ATTTAAAAC Seq ID NO: 16 DNA sequenceNucleic Acid Accession #: CAT cluster1          11         21         31         41         51|          |          |          |          |          | CTTTTTTTTTTTTTTTTTTT TAGTAGAGAC AGGGTTTCAC CATGTTAGCC AGGATGGTCT 60 CGATCTCCTGACCTCATGAT CTTCCTGCTT TGGCCTCCCA AAGTGCTGCG ATTACAGGCG 120 TGAGCCACTGCACCCAGCCC AGAGTTTTTT TTAACAAGGT TCTTCTCAGC AATTCTAGTA 180 TCCAGATATAGGCCCATCAT AGACATCACA CAAGCGTGTA CTTCATAATC CTGGTGAATA 240 CAGAAGTTTCCTGGACTCCT TGATGAGCTA CTGCTTTCGC TCCTATATCA GTGTTTTCAG 300 CTGATGTCATTTGTGATTGT GTTTCTGACT TTCTGTAGGC AGAAAAAAAC TTTCATTTTT 360 TTTTTGCTTACATGCACATA AATGTAAGCG CTAATTCTTA TATTAAACTG TTTATTTCTA 420 TAATACTTAATTGGCTGTTT TCCTGGCTGA ACCAAACCAA GAGCATAAGG AATGATAACC 480 TTCAAAACTGATTAAATTAG AGATCAATAA ATGGAGCTGT TTTAATTCTA TTATTCTTCT 540 TTCATAGATTAAATAGAAAA TTTTT Seq ID NO: 17 DNA sequence Nucleic Acid Accession #:CAT cluster 1          11         21         31         41         51|          |          |          |          |          | GGCACGAGAAGACGCCACAT CCCCTATTAT AGAATAGCTA ATAAATTTCC ATGATCACAC 60 ACTAATAATTGTTTTCCTAA TTAGCTCCTT AGTCCTCTAT ATCATCTCGC TAATATTAAC 120 AACAAAACTAACACATACAA GCACAATAGA TGCACAATAA GTTGAAACCA TTTGAACTAT 180 TCTACCAGCTGTAATCCTTA TCATAATTGC TCTCCCCTCT CTACGCATTC TATATATAAT 240 AGACGAAATCAACAACCCCG TATTAACCGT TAAAACCATA GGGCACCAAT GATACTGAAG 300 CTACGAATATACTGACTATG AAGACCTATG CTTTGATTCA TATATAATCC CAACAAACGA 380 CCTAAAACCTGGTGAACTAC GACTGCTAGA AGTTGATAAC CGAGTCGTTC TGCCAATAGA 420 ACTTCCAATCCGTATATTAA TTTCATCTGA AGACGTCCTC CACTCATGAG CAGTCCCCTC 480 CCTAGGACTTAAAACTGATG CCATCCCAGG CCGACTAAAT CCAGCACAGT ACATCAACCG 540 ACCAGGGTTATTCTATGGCC AATGTCTGAA TTTGTGGTCT TACCATAGCT TTTTGCCATT 600 GTCCTAGAATGGGTCCCTAA AATATTTCGG NACTGGTCTG Seq ID NO: 18 DNA sequence Nucleic AcidAccession #: CAT cluster1          11         21         31         41         51|          |          |          |          |          | GTGTACATCAGAGCAAAAAT ACAGAGTATT TATTCATTTC TTCCCACTAG AGGGACACAC 60 TGTTCTTGGACAGACAAATG AATCATCAGT TGTCAGGAGT TGCCTTTGGA GAATGATCAA 120 TGAACTCCTTTTCAGGGGTT GGAAATTGAT ACCAGGGTCC ATCACCTCGG GCACGCATCA 180 GCCTTCGAACTTCCTGCTCC TTTAACCGTA ACTCAGCCTT TTCAGATTCA ATCTGGAGGA 240 TAGCCAGGGTTTTCTCGTAG TTCTTTTCAG GGCCATCATA GAAATTCCGG GCGATCCATC 300 TTGATATCGGATGCTTGTAA TACTCCCAGT GTTCAGGGAT GTAGCCTTCT GGGATTTCTG 360 CAAGCTCGGCTTCACCAATA AATATGTTCA CCAGTGTTAT GCCAATTATA ACTGGGATCC 420 CAGTCAACATAAGGTAGAAT TTCATTAACC TCAAGAAGCG AGCGTCATAG TATAAAGAAG 480 GCTTGACGACAAACAGTCTC TTGCCATGTC CCCACTGTGC COCACAGGAG CGACAGTCTT 540 CGGAAANTCCGCGTGAGAAA ACTTCCGACT CCGAGTCTAG GACCAGCGCG GCGGCAAGAC 600 CACGCTGTCAGCGCGGAGAC CGAANCCGCT GCAGCAGCTC ATGGCCGCCA TGG Seq ID ND: 19 DNAsequence Nucleic Acid Accession #: CAT cluster1          11         21         31         41         51|          |          |          |          |          | TAGTCCAGTNAATTACTTTA ATTTCGCTTT TCCATAATAC TGGTATTCCA TAGAAGAAAA 60 TCTTTTATTAATATTCTATA CTACTACATC CGACACCAGA TGACTAAAGT TTGCAATGGT 120 CCAAAATTCTGTAAACCCAT TAAATDCAAT TCATACTTTA TTTTGGCAGT ATTCATTTCA 160 TCATTACTTTATTTGGATGC TAACGCAAGT ACTTCTAAGG AAAAGCTGTC ATATAATTAC 240 TTTAGTCAAGCATTCAGTAG AGGCAATAAT CAAACCTCTA TCCCAACATT TTACACTTGT 300 AACAGAATGAAGGATGAGGT ACAACATACA TTTTTGGCAA TTTACTATTA AGGGCCATAA 360 TCATTTTAGGGGCGCTTAGG GCCCATATAT ATATATATAT ATTTTTGGAC A Seq ID NO: 20 DNA sequenceNucleic Acid Accession #: U92072 Coding sequence: 351..37011          11         21         31         41         51|          |          |          |          |          | CCCGGGCGGCTGCGCTGAGC AGAGGCCCAG CCCGGGACGC GCCGAGGGAC TGCGGGGCTG 60 CGGGTCATGGATGCGGCGGC AGCGGCGCGG GACGGCCGGA GCCCGGCCGC GACCAGGTGA 120 GGAGGCGGCGTCCGGCGCCA CTGCAGCCGC AGCGGCCTCG GAGGAAGAGG GCTCGCCGCC 180 GCGCGCCCGCCCGCCGTCTC TGCCCTTCCT GTTGGGATTA TCTTCTGCTC CCCGCTGCTT 240 CTTCGCTCCCCGCGGTCGAA GCCGCCTCTA GGCTTCAGCG GCTCGGACTC CTTGGCAGCC 300 GGTGCCTCTGCTACCTGGGC CTCGTAGCTG GGAGACCCTT GGGCGAGACC ATGAGGAAAT 360 TCAACATCAGGAAGGTGCTG GACGGCCTGA CCGCAGTCTC GTCCTCGGCC TCGCAACAGC 420 AGCAACAGCAGCAGCACCCG CCTGGGAACC GGGAGCCCGA GATCCAGGAG ACGCTCCAGT 480 CCGAGCACTTCCAACTCTGC AAGACTGTTC GCCATGGATT TCCCTATCAG CCCTCAGCCC 540 TGGCCTTTGATCCCGTTCAG AAGATCCTGG CGGTAGGAAC CCAGACTGGT GCTTTAAGGC 600 TCTTTGGTCGTCCAGGGGTG GAATGTTATT GCCAGCACGA CAGCGGAGCG GCAGTGATTC 660 AACTCCAGTTCCTGATTAAT GAGGGAGCCC TTGTGAGTGC CTTGGCTGAT GACACCTTAC 720 ACTTGTGGAATTTACGTCAG AAAAGGCCTG CTGTGCTACA TTCACTCAAA TTTTGCAGAD 780 AAAGGGTTACATTTTGCCAT CTGCCTITCC AGAGTAAGTG GCTCTATGTG GGCACGGAAC 840 GAGGTAATATACATATTGTC AATGTGGAGT CCTTCACACT CTCAGGCTAC QTCATTATGT 900 GGAATAAAGCCATCGAACTG TCATCTAAAT CTCACCCAGG ACCTGTTGTC CATATAAGTG 960 ATAATCCCATGGACGAGGGG AAGCTTCTGA TTGGCTTTGA ATCTGGAACA GTAGTCTTAT 1020 GGGACCTTAAGTCAAAGAAG GCTGACTACA GATACACTTA CGACGAGGCT ATTCACTCTG 1080 TGGCTTGGCATCATGAAGGA AAACAGTTTA TTTGCAGTCA TTCTGATGGT ACATTGACCA 1140 TATGGAATGTGAGGTCCCCT ACTAAACCTG TACAGACCAT CACTCCTCAC GGAAAACAGT 1200 TAAAGGATGGGAAGAAACCC GAGCCGTGCA AGCCTATCCT CAAGGTGGAG TTCAAGACAA 1260 CAAGATCGGGGGAACCTTTT ATTATTTTGT CGGGAGGCTT ATCATATGAT ACCGTGGGAA 1320 CAAGACCTTGCTTAACAGTG ATGCATCGGA AAAGCACGGC AGTGCTGGAA ATGGACTATT 1380 CAATTGTCGACTTTCTCACA CTCTGTGAAA CGCCATATCC AAATGATTTT CAGGAGCCGT 1440 ATGCTGTGGTTGTTCTCCTG GAGAAGGATT TAGTGCTGAT AGACCTGGCA CAGAATGGAT 1500 ACCCTATATTTGAGAATCCC TACCCTTTGA GTATACACGA GTCCCCTGTT ACATGTTGTG 1560 AATATTTTGCTGATTGTCCT GTGGACCTTA TTCCTGCACT TTATTCTGTT GGAGCTAGAC 1620 AGAAACGTCAAGGTTACAGC AAAAAGGAAT GGCCCATCAA TGGTGGTAAT TGGGGCTTGG 1680 GTGCTCAAAGTTACCCAGAA ATAATTATTA CAGGGCATGC TGATGGCTCA ATTAAATTCT 1740 GGGATGCTTCTGCAATAACT CTACAAGTAC TGTATAAATT AAAAACATCT AAAGTATTTG 1800 AAAAGTCAAGAAATAAAGAT GACAGACAGA ACACCGACAT TGTAGATGAA GATCCATATG 1880 CCATTCAGATCATCTCCTGG TGCCCAGAGA GCAGAATGCT GTGCATAGCC GGAGTGTCGG 1920 CTCATGTCATCATTTATAGA TTCAGCAAGC AGGAAGTGGT TACAGAAGTC ATCCCGATGC 1980 TTGAAGTCCGACIGTTATAT GAAATAAATG ATGTGGAAAC GCCGGAGGGT GAGCAGCCAC 2040 CCCCTTTGTCCACTCCCGTG GGCAGCTCCA CCTCTCAGCC CATCCCCCCT CAGTCTCATC 2100 CGTCTACCAGCAGCAGCTCA TCGGACGGGC TTCGAGATAA TGTACCGTGT TTAAAAGTTA 2180 AAAACTCACCACTTAAACAG TCTCCCGGCT ATCAAACAGA GCTAGTCATC CAGTTGGTGT 2220 GGGTGGGTGGACAACCCCCG CAGCAGATCA CCAGCCTAGC ACTCAACTCT TCCTACGGAT 2280 TGGTGGTTTTGGGCAACTCC AATGGCATTG CAATGGTTGA CTACCTCCAG AAAGCAGTGC 2140 TGCTCAACCTCAGCACCATT GAACTATACG GCTCAAATGA TCCTTATCGG AGAGAACCGA 2400 GGTCGCCCCGCAAATCTCGA CAGCCTTCAG GAGCGGGCCT GTGTGATATT ACCGAAGGAA 2460 CTGTCGTCCCAGAGGATCGC TGCAAATCTC CGACTTCCGC AAAGATGTCA AGGAAATTAA 2520 GCTTGCCAACTGATCTAAAG CCTGATTTAG ATGTGAAAGA CAATTCCTTC AGCAGATCTC 2580 GGAGTTCAAGTGTGACCAGC ATTGACAAAG AGTCCCGGGA AGCCATTTCT GCTCTTCATT 2640 TCTGTGAGACTTTCACAAGG AAGGCAGACT CCTCCCCCTC CCCGTGCCTG TGGGTGGGAA 2700 CCACAGTGGGAACTGCCTTT GTCATCACGC TGAATCTCCC CCTGGGGCCT GAGCAGAGAC 2760 TGCTTCAGCCAGTGATTGTG TCTCCAAGCG GTACTATATT GAGGTTAAAA GGTGCGATCT 2820 TGAGAATGGCATTTCTGGAT GCCGCGGGCT GCTTAATGCC ACCTGCATAC GAACCCTGGA 2880 CAGAGCACAACGTTCCTGAA GAAAAAGACG AAAAGGAGAA ATTGAAAAAG CGGCGACCTG 2940 TCTCAGTGTCCCCCTCCTCT TCTCAGGAAA TTAGTGAAAA CCAGTACGCA GTGATATGTT 3000 CTGAAAAGCAAGCAAAGGTC ATCTCACTGC CAACCCAGAA CTGTGCATAC AAGCAGAACA 3080 TCACTGAGACGTCCTTCGTG CICCGTGGAG ACATTGTCGC CCTGAGTAAC AGTGTCTGCC 3120 TCGCCTGCTTCTGTGCCAAC GGCCACATTA TGACTTTCAG TTTGCCGAGC TTGAGGCCTC 3180 TGCTGGATGTCTACTACCTG CCCCTTACCA ACATGCGGAT AGCCAGGACA TTCTGCTTCG 3240 CCAACAGTGGGCAAGCCTTA TACCTTGTTT CACCTACCGA AATCCAGAGA CTCACCTACA 3300 GTCAGGAGACGTGTGAAAAC CTTCAGGAGA TGCTTGGTGA GCTCTTCACG CCTGTAGAAA 3360 CACCAGAAGCACCAAACAGA GGGTTCTTCA AAGGCTTATT TGGAGGTGGT GCACAATCTC 3420 TTGATAGAGAACAACTGTTT GGAGAGTCAT CCTCGGGAAA GGCGTCAAGG AGCCTTGCAC 3480 AGCACATCCCGGGTCCTGGC GGGATCGAAG GTGTGAAGGG AGCCGCGTCG GGAGTGGTGG 3540 GAGAACTGGCCCGAGCCAGG CTGGCCCTCG ACGAAAGAGG ACAGAAGCTC AGCGACTTGG 3600 AAGAGAGGACTGCAGCCATG ATGTCCAGTG CAGACTCGTT TTCCAAACAT GCTCATGAGA 3660 TGATGCTGAAATACAAAGAT AAGAAGTGGT ACCAGTTCTG ACAAGTAGCA CTCAGTAAGT 3720 CCAGCTTCAACCAGAAGGAA AAAGACGTTT CCTTGTTGAG GTCACTGATG TATTTGGGAA 3780 AGATAACATAAAAGGGATGC ACACTGCTGA CAGCGTCTTT CCCAGCACAA TCATGCACTT Seq ID NO: 21Protein sequence Protein Accession #: AAD047561          11         21         31         41         51|          |          |          |          |          | MRKFNIRKVLDGLTAGSSSA SQQGGQQQNP PGNREPEIQE TLQSEHFQLC ETVRNGPPYQ 60 PSALAFDPVQKILAVGTQTG ALRLFGPPGV ECYCQHDSGA AVIQLGFLIN EGALVSALAD 120 DTLHLWNLRQKRPAVLHSLK FCRERVTFCH LPFQSKWLYV GTERGNINIV NVESFTLSGY 180 VIMWNKAIELSSKSHPGPVV HISDNPMDEG ELLIGFESGT VVLWDLKSKK AnYRYTYGSA 240 IHSVAWHHEGKQFICSHSDG TLTIWNVRSP TKPVQTGTPN GKQLIGGKKP ESCEPILEVE 300 FKTTRSGEPPTILSGGLSYD TVGRRPCLTV MHGKSTAVLE MGYSIVGELT LCETPYPNDF 360 QEPYAVVVLLEKDLVLIDLA GNGYPIFENP YPLSIHESPV TCCEYFADCP VDLIPALYSV 420 CARQKRQGYSKEEMPINGGN WGLGAQSYPE IIITGHADGS IKFWDASAIT LQVLYKLKTS 480 KVFEKSRNKDDRQNTDIVDE DPYAIQIISW CRESRELCIA GVSAHVIIYR FSRQEVVTEV 540 IPMLEVRLLYEINDVETPEG EQPPPLSTPV GSSTSQPIPP QSHPSTSSSS SDGLRDNVPC 600 LKVKNSPLKQSPGYQTELVI QLVWVGGEPP QQITSLALNS SYGLVVFGNS NGIAMVDYLG 660 KAVLLNLSTISLYGSNDPYR REPRSPSKSR QPSGAGLGDI TEGTVVPEDR CKSPTSARES 720 RKLSLPTDLKPGLDVKDNSF SRSRSSSVTS IDEESREAIS ALHPCETFTR KADSSPSPCL 780 WVGTTVGTAFVITLNLPLGP EQRLLQPVIV SPSGTGLRLE GAILRMASLD AAGCLMPPAY 840 EPWTEHNVPEEKDEKEKLKE RRPVSVSPSS SQEISENQYA VICSEKQAKV ISLPTQNCAY 900 KQNITETSFVLEGGIVALSE SVCLACFCAN GHIMTFSLPS LRPLLDVYYL PLTNNRIART 960 ECEANSGQALYLVSPTEIQR LTYSQETCEN LQEMLGELET PVETPEAPNR CFFKGLFGGG 1020 AQSLDREELFGESSSGKASR SLAQNGPGPG GIEGVKGAAS GVVGELAPAR LALDERGQEL 1080 SDLEERTAAMMSSADSFSKH AHEMNLKYKD KEWYQE Seq ID NO 22 DNA sequence Nucleic AcidAccession #: CAT cluster1          11         21         31         41         51|          |          |          |          |          | TCCCATCGGGTGAACCGTGG TCTTGTTCCG TCCGCCCACA ATCGCTCTCC AGCTTTGACG 60 CCCCCGGCAAAGCCIGGCTC GTTCACAGCT CTCTCGCACC TCCTGGAGCT TCAGCTTCTT 120 CCGTTGCAGAGAAGCTTTAT GGGCCAATTC GTTCGGCATC CCGGGGGCAG GTGCGCGGTG 180 CGCGGGGAAGAAGAGGATTT GACTGCGGTT CTCCACCCCC GGCGCCCAAC CTCCACCCCG 240 GTGCGCGCGCTCTTCCAGGC TCCTGCTGGT CCCACTTGCC AGGAGTTAGG TCTCAGGTCA 300 GCCTGAGCTCCTGAGACGCC CACGCCCGGA AAGACACGTA GGGGAAACCA TCTGCTCACT 360 TCTGTCCTGTCCGGAAGGGA TCCCTTTCTG ACGGGAAAGA AAGGCGCTAA ACAAGCACTG 420 GCCTTGAGATAAGCAATGCT GAAGCACTTG CAGCTCACCT ATTACCATAA ACTGACTGAG 480 CCCTCCCTACACAAGCCGTA ACTACTGCTT TGATTGGACA AGAGATTGAT TTCAGTAGTT 540 TTCTCTTGATAAGAGACCAC TGGCCGTGGG CGGGTTCTGG ACAGTTTACA GAAGCTATGC 600 ACTTGATTGCCTTTGTGTCC CTGCTTCACC TTTTGAAGCA TAGGGCCTAA TTATAATGTA 860 TTTAAATGTTGTCTCCACCC CAAAGTGAAC ATGGGTTGCA TGTAACAGGC ATGTTTACTC 720 AGCATGCATGCAGCAGGATC CCTTCACAAA TATTCAGAGC TCCCCCTATT CCCTGTTGAA 780 TATGTATATGTGGCCAGCCA GATCAACGTA AATCACTATT CGCCCTCCCC TCCCTGGAAA 840 CCTACTTTTCGGGTTTCAGC AGGAAGCTAT GCCTCCCAGG CTTGTCGAAG AGGGCCCATT 900 TTCGGGCTTGATAACCCCTT TATAAAAAAA TAAAATCTCC TTTCTAAATT TAAAATACAA 960 CCACACCACCGGCCCGCAAC TATTGGGGGG GAAAAAGAAT GAAGACACAC GGTACATAGT 1020 TTCATGCACATTGTTAAGGA GACAGGTGCC CCCAAGCAGG COGACATCAC GCAGTACGCA 1080 GCTTGAGCATGCCGAAGACG CGAGCGACTC ATAGAACACG ACGACGCTCG CAAGGCACTA 1140 AGCATAGCTACTACCACTCG TCGAAGAGTC ATACACAGAT TTCTATTGGC GA Seq ID NO 23 DNA sequenceNucleic Acid Accession #: CAT cluster1          11         21         31         41         51|          |          |          |          |          | CTATGAATCTCGGAAATTAC TCAAACCATC AGCCTCTGCA AGAAGCAAAG TGGACGGCCG 60 GGCGCGGTGGCTCACTCCTG GAATCCCAGC ACTTTGGGAG CCCGAGGTGG CGGGATCACG 120 AGGTCAGGAGATCGAGACTG TTCTGGCTAA ACCAGTGAAA CCCCCTCTCT ACTAAAAAAA 180 TAAGAAAAGCGAAGTGCATC TCCCATAAAC GAGGTACTGC AGGAAGAAAG CAGAAAATGA 240 GACCCGAGTACACACATGCA CGCGGGCGCC GCACACACAC ACCAGAAGAA ATGAACCAAG 300 AGGAAAGGAAACATTTTCAA ATAAGCATTT GGAGATOGGA AAAACACCTT GAAACAGAAA 360 TTCATAAAGTACAGAATTTT TTTTTAAGTT AAAAAAGGAA CAATAATAGA CAGAAAATGA 420 ATGAAAAATTAAATGTCATA TCAGAAGTGA AGATAAATTA AAAGTGGTCA AAGGAGAAGA 480 GATCTAAATGCAAACTTAAG AAGGGGCAAT TTTTTTTTTT TTTTTTTTTG AGACGCAGCC 640 TCACTCTGTC GCSeq ID NO: 24 DNA sequence Nucleic Acid Accession #: NM_000044.1 Codingsequence: 1115..38741          11         21         31         41         51|          |          |          |          |          | CGAGATCCCGGGGAGCCAGC TTGCTGGGAG AGCGGGACGG TCCGGAGCAA GCCCACAGGC 60 AGAGGAGGCGACAGAGGGAA AAAGGGCCGA GCTAGCCGCT CCAGTGCTGT ACAGGAGCCG 120 AAGGGACGCACCACGCCAGC CCCAGCCCGG CTCCAGCGAC AGCCAACGCC TCTTGCAGCG 180 CGGCGGCTTCGAAGCCGCCG CCCGGAGCTG CCCTTTCCTC TTCGGTGAAG TTTTTAAAAG 240 CTGCTAAAGACTCGGAGGAA GCAAGGAAAG TGCCTGGTAG GACTGACGGC TGCCTTTGTC 300 CTCCTCCTCTCCACCCCGCC TCCCCCCACC CTGCCTTCCC CCCCTCCCCC GTCTTCTCTC 360 CCGCAGCTGCCTCAGTCGGC TACTCTCAGC CAACCCCCCT CACCACCCTT CTCCCCACCC 420 GCCCCCCCGCCCCCGTCGGC CCAGCGCTGC CAGCCCGAGT TTGCAGAGAG GTAACTCCCT 480 TTGGCTGCGAGCGGGCGAGC TAGCTGCACA TTGCAAAGAA GGCTCTTAGG AGCCAGGCGA 540 CTGGGGAGCGGCTTCAGCAC TGCAGCCACG ACCCGCCTGG TTAGAATTCC GGCGGAGAGA 600 ACCCTCTGTTTTCCCCCACT CTCTCTCCAC CTCCTCCTGC CTTCCCCACC CCGAGTGCGG 660 AGCAGAGATCAAAAGATGAA AAGGCAGTCA GGTCTTCAGT AGCCAAAAAA CAAAACAAAC 720 AAAAACAAAAAAGCCGAAAT AAAAGAAAAA GATAATAACT CAGTTCTTAT TTGCACCTAC 780 TTCAGTGGACACTGAATTTG GAAGGTGGAG GATTTTGTTT TTTTCTTTTA AGATCTGGGC 840 ATCTTTTGAATCTACCCTTC AAGTATTAAG AGACAGACTG TGAGCCTAGC AGGGCAGATC 900 TTGTCCACCGTGTGTCTTCT TCTGCACGAG ACTTTGAGGC TGTCAGAGCG CTTTTTGCGT 1020 ACTACCGCATCATCACAGCC TGTTGAACTC TTCTGAGCAA GAGAAGGGGA GGCGGGGTAA 1080 GGGAAGTAGGTGGAAGATTC AGCCAAGCTC AAGGATGGAA GTGCAGTTAG GGCTGGGAAG 1140 GGTCTACCCTCGGCCGCCGT CCAAGACCTA CCGAGGAGCT TTCCAGAATC TGTTCCAGAG 1200 CGTGCGCGAAGTGATCCAGA ACCCGGGCCC CAGGCACCCA GAGGCCGCGA GCGCAGCACC 1260 TCCCGGCGCCAGTTTGCTGC TGCTGCAGCA GCAGCAGCAG CAGCAGCAGC AGCAGCAGCA 1320 GCAGCAGCAGCAGCAGCAGC AGCAGCAAGA GACTAGCCCC AGGCAGCAGC AGCAGCAGCA 1380 GGGTGAGGATGGTTCTCCCC AAGCCCATCG TAGAGGCCCC ACAGGCTACC TGGTCCTGGA 1440 TGAGGAACAGCAACCTTCAC AGCCGCAGTC GGCCCTGGAG TGCCACCCCG AGAGAGGTTG 1500 CGTCCCAGAGCCTGGAGCCG CCGTGGCCGC CAGCAAGGGG CTGCCGCAGC AGCTGCCAGC 1560 ACCTCCGGACGAGGATGACT CAGCTGCCCC ATCCACGTTG TCCCTGCTGG GCCCCACTTT 1620 CCCCGGCTTAAGCAGCTGCT CCGCTGACCT TAAAGACATC CTGAGCGAGG CCAGCACCAT 1680 GCAACTCCTTCAGCAACAGC AGCAGGAAGC AGTATCCGAA GGCAGCAGCA GCGGAGGAGC 1740 GAGGGAGGCCTCGGGGGCTC CCACTTCCTC CAAGGACAAT TACTTAGGGG GCACTTCGAC 1800 CATTTCTGACAACGCCAAGG AGTTGTGTAA GGCAGTGTCG GTGTCCATGG GCCTGGGTGT 1860 GGAGGCGTTGGAGCATCTGA GTCCAGGGGA ACAGCTTCGG GGGGATTGCA TGTACGCCCC 1920 ACTTTTGGGAGTTCCACCCG CTGTGCGTCC CACTCCTTGT GCCCCATTGG CCGAATGCAA 1980 AGGTTCTCTGCTAGACGACA GCGCAGGCAA GAGCACTGAA GATACTGCTG AGTATTCCCC 2040 TTTCAAGGGAGGTTACACCA AAGGGCTAGA AGGCGAGAGC CTAGGCTGCT CTGGCAGCGC 2100 TGCAGCAGGGAGCTCCGGGA CACTTGAACT GCCGTCTACC CTGTCTCTCT ACAAGTCCGG 2160 AGCACTGGACGAGGCAGCTG CGTACCAGAG TCGCGACTAC TACAACTTTC CACTGGCTCT 2220 GGCCGGACCGCCGCCCCCTC CGCCGCCTCC CCATCCCCAC GCTCGCATCA AGCTGGAGAA 2280 CCCGCTGGACTACGGCAGCG CCTGGGCGGC TGCGGCGGCG CAGTGCCGCT ATGGGGACCT 2340 GGCGAGCCTGCATGGCGCGG GTGCAGCGGG ACCCGGTTCT GGGTCACCCT CAGCCGCCGC 2400 TTCCTCATCCTGGCACACTC TCTTCACAGC CGAAGAAGGC CAGTTGTATG GACCGTGTGG 2460 TGGTGGTGGGGGTGGTGGCG GCGGCGGCGG CGGCGGCGGC GGCGGCGGCG GCGGCGGCGG 2520 CGGCGGCGGCGAGGCGGGAG CTGTAGCCCC CTACGGCTAC ACTCGGCCCC CTCAGGGGCT 2580 GGCGGGCCAGGAAAGCGACT TCACCGCACC TGATGTGTGG TACCCTGGCG GCATGGTGAG 2640 CAGAGTGCCCTATCCCAGTC CCACTTGTGT CAAAAGCGAA ATGGGCCCCT GGATGGATAG 2700 CTACTCCGGACCTTACGGGG ACATGCGTTT GGAGACTGCC AGGGACCATG TTTTGCCCAT 2760 TGACTATTACTTTCCACCCC AGAAGACCTG CCTGATCTGT GGAGATGAAG CTTCTGGGTG 2820 TCACTATGGAGCTCTCACAT GTGGAAGCTG CAAGGTCTTC TTCAAAAGAG CCGCTGAAGG 2880 GAAACAGAAGTACCTGTGCG CCAGCAGAAA TGATTGCACT ATTGATAAAT TCCGAAGGAA 2940 AAATTGTCCATCTTGTCGTC TTCGGAAATG TTATGAAGCA GGGATGACTC TGGGAGCCCG 3000 GAAGCTGAAGAAACTTGGTA ATCTGAAACT ACAGGAGGAA GGAGAGGCTT CCAGCACCAC 3060 CAGCCCCACTGAGGAGACAA CCCAGAAGCT GACAGTGTCA CACATTGAAG GCTATGAATG 3120 TCAGCCCATCTTTCTGAATG TCCTGGAAGC CATTGAGCCA GGTGTAGTGT GTGCTGGACA 3180 CGACAACAACCAGCCCGACT CCTTTGCAGC CTTGCTCTCT AGCCTCAATG AACTGGGAGA 3240 GAGACAGCTTGTACACGTGG TCAAGTGGGC CAAGGCCTTG CCTGGCTTCC GCAACTTACA 3300 CGTGGACGACCAGATGGCTG TCATTCAGTA CTCCTGGATG GGGCTCATGG TGTTTGCCAT 3360 GGGCTGGCGATCCTTCACCA ATGTCAACTC CAGGATGCTC TACTTCGCCC CTGATCTGGT 3420 TTTCAATGAGTACCGCATGC ACAAGTCCCG GATGTACAGC CAGTGTGTCC GAATGAGGCA 3480 CCTCTCTCAAGAGTTTGGAT GGCTCCAAAT CACCCCCCAG GAATTCCTGT GCATGAAAGC 3540 ACTGCTACTCTTCAGCATTA TTCCAGTGGA TGGGCTGAAA AATCAAAAAT TCTTTGATGA 3600 ACTTCGAATGAACTACATCA AGGAACTCGA TCGTATCATT GCATGCAAAA GAAAAAATCC 3660 CACATCCTGCTCAAGACGCT TCTACCAGCT CACCAAGCTC CTGGACTCCG TGCAGCCTAT 3720 TGCGAGAGAGCTGCATCAGT TCACTTTTGA CCTGCTAATC AAGTCACACA TGGTGAGCGT 3780 GGACTTTCCGGAAATGATGG CAGAGATCAT CTCTGTGCAA GTGCCCAAGA TCCTTTCTGG 3840 GAAAGTCAAGCCCATCTATT TCCACACCCA GTGAAGCATT GGAAACCCTA TTTCCCCACC 3900 CCAGCTCATGCCCCCTTTCA GATGTCCTCT GCCTGTTATA ACTCTGCACT ACTCCTCTGC 3960 AGTGCCTTGGGGAATTTCCT CTATTGATGT ACAGTCTGTC ATGAACATGT TCCTGAATTC 4020 TATTTGCTGGGCTTTTTTTT TCTCTTTCTC TCCTTTCTTT TTCTTCTTCC CTCCCTATCT 4080 AACCCTCCCATGGCACCTTC AGACTTTGCT TCCCATTGTG GCTCCTATCT GTGTTTTGAA 4140 TGGTGTTGTATGCCTTTAAA TCTGTGATGA TCCTCATATG GCCCAGTGTC AAGTTGTGCT 4200 TGTTTACAGCACTACTCTGT GCCAGCCACA CAAACGTTTA CTTATCTTAT GCCACGGGAA 4260 GTTTAGAGAGCTAAGATTAT CTGGGGAAAT CAAAACAAAA AACAAGCAAA CAAAAAAAAA 4320 A Seq ID NO:25 Protein Sequence Protein Accession #: NP_000035.11          11         21         31         41         51|          |          |          |          |          | MEVQLGLGRVYPRPPSKTYR GAFQNLFQSV REVIQNPGPR HPEAASAAPP GASLLLLQQQ 60 QQQQQQQQQQQQQQQQQQET SPRQQQQQQG EDGSPQAHRR GPTGYLVLDE EQQPSQPQSA 120 LECHPERGCVPEPGAAVAAS KGLPQQLPAP PDEDDSAAPS TLSLLGPTFP GLSSCSADLK 180 DILSEASTMQLLQQQQQEAV SEGSSSGRAR EASGAPTSSK DNYLGGTSTI SDNAKELCKA 240 VSVSMGLGVEALEHLSPGEQ LRGDCMYAPL LGVPPAVRPT PCAPLAECKG SLLDDSAGKS 300 TEDTAEYSPFKGGYTKGLEG ESLGCSGSAA AGSSGTLELP STLSLYKSGA LDEAAAYQSR 360 DYYNFPLALAGPPPPPPPPH PHARIKLENP LDYGSAWAAA AAQCRYGDLA SLHGAGAAGP 420 GSGSPSAAASSSWHTLFTAE EGQLYGPCGG GGGGGGGGGG GGGGGGGGGG GGEAGAVAPY 480 GYTRPPQGLAGQESDFTAPD VWYPGGMVSR VPYPSPTCVK SEMGPWMDSY SGPYGDMRLE 540 TARDHVLPIDYYFPPQKTCL ICGDEASGCH YGALTCGSCK VFFKRAAEGK QKYLCASRND 600 CTIDKFRRKNCPSCRLRKCY EAGMTGAGRK LKKLGNLKLQ EEGEASSTTS PTEETTQKLT 660 VSHIEGYECQPIFLNVLEAI EPGVVCAGHD NNQPDSFAAL LSSLNELGER QLVHVVKWAK 720 ALPGFRNLHNDDQMAVIQYS WMGLMVFAMG WRSFTNVNSR MLYFAPDLVF NEYRMHKSRM 780 YSQCVRMRHLSQEFGWLQIT PQEFLCMKAL LLFSIIPVDG LKNQKFFDEL RMNYIKELDR 840 IIACKRKNPTSCSRRFYQLT KLLDSVQPIA RELHQFTFDL LIKSHMVSVD FPEMMAEIIS 900 VQVPKILSGKVKPIYFHTQ Seq ID NO: 26 DNA sequence Nucleic Acid Accession #: CATcluster 1          11         21         31         41         51|          |          |          |          |          | AGCATTATCCATGGCCAGTG ATTGATGGAC TTGTTGAGGT CCTATGCAGA GTGCTTCATA 60 TATCTCATCTCAATCCTCTA AATAACCATG AAAGTTGATG ATTATCTCAT GGTACAGATG 120 GGAGGCTAAGAGTGTTTAAT TTTCCCCAAG TTCCAGTGCT AGTAAGTGTT GNNNNNNNNN 180 NNTGAACTGGTGTTAATGGT GTTTCTAGTC GATGCTGTTA TCTGTTGCAC CACATTTTGA 240 ATAATCTTGGACTTTCAGAG TATGAAGGAC GATTAAATAT AACCCTTTGG TATAAATGTT 300 CTCTCTCTCGCTCCTCTGTA ACAATTGGAG AAACAGAGTT CTAACAATAT TAAAATCAGC 360 CATAGACAGAGAGTAGTGAG AAATATACTT TTTTTAATAC AGAAGGTTCC CTGAAGTACT 420 TTTAGTATTATTCTAAATTA AGCAATAACC AATGAACAAT TTTGGTCATA AGCAGTTTCT 480 CTCCAGAAAAAAAAAAAAAA AGTCGAC Seq ID NO: 27 DNA sequence Nucleic Acid Accession #:NM_006551.2 Coding sequence: 64..3361          11         21         31         41         51|          |          |          |          |          | AATTCTAGAAGTCCAAATCA CTCATTGTTT GTGAAAGCTG AGCTCACAGC AAAACAAGCC 60 ACCATGAAGCTGTCGGTGTG TCTCCTGCTG GTCACGCTGG CCCTCTGCTG CTACCAGGCC 120 AATGCCGAGTTCTGCCCAGC TCTTGTTTCT GAGCTGTTAG ACTTCTTCTT CATTAGTGAA 180 CCTCTGTTCAAGTTAAGTCT TGCCAAATTT GATGCCCCTC AACGAAGCCT CATTGCGGAA 240 TTAGGAGTGAAGAGATGCAC GGATCAGATG TCCCTTCAGA AACGAAGCCT CATTGCGGAA 300 GTCCTGGTGAAAATATTGAA GAAATGTAGT GTGTGACATG TAAAAACTTT CATCCTGGTT 360 TCCACTGTCTTTCAATGACA CCCTGATCTT CACTGCAGAA TGTAAAGGTT TCAACGTCTT 420 GCTTTAATAAATCACTTGCT CTAC Seq ID NO: 28 Protein sequence Protein Accession #:NP_006542.1 1          11         21         31         41         51|          |          |          |          |          | MKLSVCLLLVTLALCCYQAN AEFCPALVSE LLDFFFISEP LFKLSLAKFD APPEAVAAKL 60 GVKRCTDQMSLQKRSLIAEV LVKILKKCSV Seq ID NO: 29 DNA sequence Nucleic Acid Accession#: NM_002645.1 Coding sequence: 1..50611          11         21         31         41         51|          |          |          |          |          | ATGGCTCAGATATTTAGCAA CAGCGGATTT AAAGAATGTC CATTTTCACA TCCGCAACCA 60 ACAAGAGCAAAAGATGTGGA CAAAGAAGAA GCATTACAGA TGGAAGCAGA GGCTTTAGCA 120 AAACTGCAAAAGGATAGACA AGTGACTGAC AATCAGAGAG GCTTTGAGTT GTCAAGCAGC 180 ACCAGAAAAAAAGCACAGGT TTATAACAAG CAGGATTATG ATCTCATGGT GTTTCCTGAA 240 TCAGATTCCCAAAAAAGAGC ATTAGATATT GATGTAGAAA AGCTCACCCA AGCTGAACTT 300 GAGAAACTATTGCTGGATGA CAGTTTCGAG ACTAAAAAAA CACCTGTATT ACCAGTTACT 360 CCTATTCTGAGCCCTTCCTT TTCAGCACAG CTCTATTTTA GACCTACTAT TCAGAGAGGA 420 CAGTGGCCACCTGGATTACC TGGGCCTTCC ACTTATGCTT TACCTTCTAT TTATCCTTCT 480 ACTTACAGTAAACAGGCTGC ATTCCAAAAT GGCTTCAATC CAAGAATGCC CACTTTTCCA 540 TCTACAGAACCTATATATTT AAGTCTTCCG GGACAATCTC CATATTTCTC ATATCCTTTG 600 ACACCTGCCACACCCTTTCA TCCACAAGGA AGCTTACCTA TCTATCGTCC AGTAGTCAGT 660 ACTGACATGGCAAAACTATT TGACAAAATA GCTAGTACAT CAGAATTTTT AAAAAATGGG 720 AAAGCAAGGACTGATTTGGA GATAACAGAT TCAAAAGTCA GCAATCTACA GGTATCTCCA 780 AAGTCTGAGGATATCAGTAA ATTTGACTGG TTAGACTTGG ATCCTCTAAG TAAGCCTAAG 840 GTGGATAATGTGGAGGTATT AGACCATGAG GAAGAGAAAA ATGTTTCAAG TTTGCTAGCA 900 AAGGATCCTTGGGATGCTGT TCTTCTTGAA GAGAGATCGA CAGCAAATTG TCATCTTGAA 960 AGAAAGGTGAATGGAAAATC CCTTTCTGTG GCAACTGTTA CAAGAAGCCA GTCTTTAAAT 1020 AATCGAACAACTGAGCTTGC AAAAGCCCAG GGCCATATAT CTCAGAAAGA CCCAAATGGG 1080 ACCAGTAGTTTGCCAACTGG AAGTTCTCTT CTTCAAGAAG TTGAAGTACA GAATGAGGAG 1140 ATGGCAGCTTTTTGTCGATC CATTACAAAA TTGAAGACCA AATTTCCATA TACCAATCAC 1200 CGCACAAACCCAGGCTATTT GTTAAGTCCA GTCACAGCGC AAAGAAACAT ATGCGGAGAA 1260 AATGCTAGTGTGAAGGTCTC CATTGACATT GAAGGATTTC AGCTACCAGT TACTTTTACG 1320 TGTGATGTGAGTTCTACTGT AGAAATCATT ATAATGCAAG CCCTTTGCTG GGTACATGAT 1380 GACTTGAATCAAGTAGATGT TGGCAGCTAT GTTCTAAAAG TTTGTGGTCA AGAGGAAGTG 1440 CTGCAGAATAATCATTGCCT TGGAAGTCAT GAGCATATTC AAAACTGTCA AAAATGGGAC 1500 ACAGAAATTAGACTACAACT CTTGACCTTC AGTGCAATGT GTCAAAATCT GGCCCGAACA 1560 GCAGAAGATGATGAAACACC CGTGGATTTA AACAAACACC TGTATCAAAT AGAAAAACCT 1620 TGCAAAGAAGCCATGACGAG ACACCCTGTT GAAGAACTCT TAGATTCTTA TCACAACCAA 1680 GTAGAACTGGCTCTTCAAAT TGAAAACCAA CACCGAGCAG TAGATCAAGT AATTAAAGCT 1740 GTAAGAAAAATCTGTAGTGC TTTAGATGGT GTCGAGACTC TTGCCATTAC AGAATCAGTA 1800 AAGAAGCTAAAGAGAGCAGT TAATCTTCCA AGGAGTAAAA CTGCTGATGT GACTTCTTTG 1860 TTTGGAGGAGAAGACACTAG CAGGAGTTCA ACTAGGGGCT CACTTAATCC TGAAAATCCT 1820 GTTCAAGTAAGCATAAACCA ATTAACTGCA GCAATTTATG ATCTTCTCAG ACTCCATGCA 1980 AATTCTGGTAGGAGTCCTAC AGACTGTGCC CAAAGTAGCA AGAGTGTCAA GGAAGCATGG 2040 ACTACAACAGAGCAGCTCCA GTTTACTATT TTTGCTGCTC ATGGAATTTC AAGTAATTGG 2100 GTATCAAATTATGAAAAATA CTACTTGATA TGTTCACTGT CTCACAATGG AAAGGATCTT 2160 TTTAAACCTATTCAATCAAA GAAGGTTGGC ACTTACAAGA ATTTCTTCTA TCTTATTAAA 2220 TGGGATGAACTAATCATTTT TCCTATCCAG ATATCACAAT TGCCATTAGA ATCAGTTCTT 2280 CACCTTACTCTTTTTGGAAT TTTAAATCAG AGCAGTGGAA GTTCCCCTGA TTCTAATAAG 2340 CAGAGAAAGGGACCAGAAGC TTTGGGCAAA GTTTCTTTAC CTCTTTGTGA CTTTAGACGG 2400 TTTTTAACATGTGGAACTAA ACTTCTATAT CTTTGGACTT CATCACATAC AAATTCTGTT 2460 CCTGGAACAGTTACCAAAAA AGGATATGTC ATGGAAAGAA TAGTGCTACA GGTTGATTTT 2520 CCTTCTCCTGCATTTGATAT TATTTATACA ACTCCTCAAG TTGACAGAAG CATTATACAG 2580 CAACATAACTTAGAAACACT AGAGAATGAT ATAAAAGGGA AACTTCTTGA TATTCTTCAT 2640 AAAGACTCATCACTTGGACT TTCTAAAGAA GATAAAGCTT TTTTATGGGA GAAACGTTAT 2700 TATTGCTTCAAACACCCAAA TTGTCTTCCT AAAATATTAG CAAGCGCCCC AAACTGGAAA 2760 TGGGGTAATCTTGCCAAAAC TTACTCATTG CTTCACCAGT GGCCTGCATT GTACCCACTA 2820 ATTGCATTGGAACTTCTTGA TTCAAAATTT GCTGATCAGG AAGTAAGATC CCTAGCTGTG 2880 ACCTGGATTGAGGCCATTAG TGATGATGAG CTAACAGATC TTCTTCCACA GTTTGTACAA 2940 GCTTTGAAATATGAAATTTA CTTGAATAGT TCATTAGTGC AATTCCTTTT GTCCAGGGCA 3000 TTGGGAAATATCCAGATAGC ACACAATTTA TATTGGCTTC TCAAAGATGC CCTGCATGAT 3060 GTACAGTTTAGTACCCGATA CGAACATGTT TTGGGTGCTC TCCTGTCAGT AGGAGGAAAA 3120 CGACTTAGAGAAGAACTTCT AAAACAGACG AAACTTGTAC AGCTTTTAGG AGGAGTAGCA 3180 GAAAAAGTAAGGCAGGCTAG TGGATCAGCC AGACAGGTTG TTCTCCAAAG AAGTATGGAA 3240 CGAGTACAGTCCTTTTTTCA GAAAAATAAA TGCCGTCTCC CTCTCAAGCC AAGTCTAGTG 3300 GCAAAAGAATTAAATATTAA GTCGTGTTCC TTCTTCAGTT CTAATGCTGT CCCCCTAAAA 3360 GTCACAATGGTGAATGCTGA CCCTCTGGGA GAAGAAATTA ATGTCATGTT TAAGGTTGGT 3420 GAAGATCTTCGGCAAGATAT GTTAGCTTTA CAGATGATAA AGATTATGGA TAAGATCTGG 3480 CTTAAAGAAGGACTAGATCT GAGGATGGTA ATTTTCAAAT GTCTCTCAAC TGGCAGAGAT 3540 CGAGGCATGGTGGAGCTGGT TCCTGCTTCC GATACCCTCA GGAAAATCCA AGTGAAATAT 3600 GGTGTGACAGGATCCTTTAA AGATAAACCA CTTGCAGAGT GGCTAAGGAA ATACAATCCC 3660 TCTGAAGAAGAATATGAAAA GGCTTCAGAG AACTTTATCT ATTCCTGTGC TGGATGCTGT 3720 GTAGCCACCTATGTTTTAGG CATCTGTGAT CGACACAATG ACAATATAAT GCTTCGAAGC 3780 ACGGGACACATGTTTCACAT TGACTTTGGA AAGTTTTTGG GACATGCACA GATGTTTGGC 3840 AGCTTCAAAAGGGATCGGGC TCCTTTTGTG CTGACCTCTG ATATGGCATA TGTCATTAAT 3900 GGGGGTGAAAAGCCCACCAT TGCTTTTCAG TTGTTTGTGG ACCTCTGCTG TCAGGCCTAC 3960 AACTTGATAAGAAAGCAGAC AAACCTTTTT CTTAACCTCC TTTCACTGAT GATTCCTTCA 4020 GGGTTACCAGAACTTACAAG TATTCAAGAT TTGAAATACG TTAGAGATGC ACTTCAACCC 4080 CAAACTACAGACGCAGAAGC TACAATTTTC TTTACTAGGC TTATTGAATC AAGTTTGGGA 4140 AGCATTGCCACAAAGTTTAA CTTCTTCATT CACAACCTTG CTCAGCTTCG TTTTTCTGGT 4200 CTTCCTTCTAATGATGAGCC CATCCTTTCA TTTTCACCTA AAACATACTC CTTTAGACAA 4260 GATGGTCGAATCAAGGAAGT CTCTGTTTTT ACATATCATA AGAAATACAA CCCAGATAAA 4320 CATTATATTTATGTAGTCCG AATTTTGTGG GAAGGACAGA TTGAACCATC ATTTGTCTTC 4380 CGAACATTTGTCGAATTTCA GGAACTTCAC AATAAGCTCA GTATTATTTT TCCACTTTGG 4440 AAGTTACCAGGCTTTCCTAA TAGGATGGTT CTAGGAAGAA CACACATAAA AGATGTAGCA 4500 GCCAAAAGGAAAATTGAGTT AAACAGTTAC TTACAGAGTT TGATGAATGC TTCAACGGAT 4560 GTAGCAGAGTGTGATCTTGT TTGTACTTTC TTCCACCCTT TACTTCGTGA TGAGAAAGCT 4620 GAAGGGATAGCTAGGTCTGC AGATGCAGGT TCCTTCAGTC CTACTCCAGG CCAAATAGGA 4680 GGAGCTGTGAAATTATCCAT CTCTTACCGA AATGGTACTC TTTTCATCAT GGTGATGCAT 4740 ATCAAAGATCTTGTTACTGA AGATGGAGCT GACCCAAATC CATATGTCAA AACATACCTA 4800 CTTCCAGATAACCACAAAAC ATCCAAACGT AAAACCAAAA TTTCACGAAA AACGAGGAAT 4860 CCGACATTCAATGAAATGCT TGTATACAGT GGATATAGCA AAGAAACCCT AAGACAGCGA 4920 GAACTTCAACTAAGTGTACT CAGTGCAGAA TCTCTGCGGG AGAATTTTTT CTTGGGTGGA 4980 GTAACCCTGCCTTTGAAAGA TTTCAACTTG AGCAAAGAGA CGGTTAAATG GTATCAGCTG 5040 ACTGCGGCAACATACTTGTA A Seq ID NO: 30 Protein sequence Protein Acceseion #:NP_002636.1 1          11         21         31         41         51|          |          |          |          |          | MAQIFSNSGFKECPFSHPEP TRAKDVDKEE ALQMEAEALA KLQKDRQVTD NQRGFELSSS 60 TRKKAQVYNKQDYDLMVFPE SDSQKRALDI DVEKLTQAEL EKLLLDSSFE TKKTPVLPVT 120 PILSPSFSAQLYFRPTIQRG QWPPGLPGPS TYALPSIYPS TYSKQAAPQN GFNPRMPTFP 180 STEPIYLSLPGQSPYPSYPL TPATPPNPQG SLPIYRPVVS TDMAKLFDKI ASTSEPLKNG 240 KARTDLEITDSKVSNLQVSP KSEDISKFDW LDLDPLSKPK VDNVEVLDHE EEKNVSSLLA 300 KDPWDAVLLEERSTANCNLE RKVNGKSLSV ATVTRSQSLN IRTTQLAKAQ GHISQKDPNG 360 TSSLPTGSSLLQEVEVQNEE MAAFCRSITR LKTKFPYTNH RTNPGYLLSP VTAQRNICGE 420 NASVKVSIDIEGFQLPVTFT CDVSSTVEII IMQALCWVHD DLNQVDVGSY VLKVCGQEEV 480 LQNNNCLGSNEHIQNCRKWD TEIRLQLLTF SANCQNLART AEDDETPVDL NKNLYQIEKP 540 CKEAMTRHPVEELLDSYHNQ VELALQIENQ HEAVDQVIKA VRKICSALDG VETLAITESV 600 KKLKRAVNLPRSKTAGVTSL FGGEDTSRSS TRGSLNPENP VQVSINQLTA AIYDLLELNA 660 NSGRSPTDCAQSSKSVKEAW TTTEQLQFTI FAANGISSNW VSNYEKYYLI CSLSNNGKDL 720 FKPIQSKKVGTYKNFFYLIK WDELIIFPIQ ISQLPLESVL HLTLFGILNQ SSGSSPDSNK 780 QRKGPEALGKVSLPLCDFRR FLTCGTKLLY LWTSSHTNSV PGTVTKKGYV MERIVLQVDP 840 PSPAFDIIYTTPQVDRSIIQ QINLETLEND IKGKLLDILN KDSSLGLSKE DKAFLWEKRY 900 YCFKHPNCLPKOLASAPNNK WGNLAKTYSL LHQWPALYPL IALELLDSKF ADQEVRSLAV 960 TWIEAISDDELTDLLPQFVQ ALKYEIYLNS SLVQFLLSRA LGNIQIAHNL YWLLKDALND 1020 VQFSTRYENVLGALLSVGGK RLREELLKQT KLVQLLGGVA EKVRQASGSA RQVVLQRSME 1080 RVQSFFQKNKCRLPLKPSLV AKELNIKSCS PFSSNAVPLK VTMVNADPLG EEINVMFKVG 1140 EDLPQDMLALQMIKIMDKIW LKEGLDLRNV IFKCLSTGRD RGMVELVPAS DTLRKIQVEY 1200 GVTGSFKDKPLAEWLRKYNP SEEEYEKASE NFIYSCAGCC VATYVLGIGD RHNDNIMLRS 1260 TGNMFHIDPGKFLGNAQMPG SFKRDRAPFV LTSDMAYVIN GGEKPTIRFQ LFVDLCCQAY 1320 NLIRKQTNLPLNLLSLMIPS GLPELTSIQD LKYVRDALQP QTTDAEATIF FTELIESSLG 1380 SIATKFNFFIHNLAQLRFSG LPSNDEPILS FSPKTYSFRQ DGRIKEVEVE TYNKKYNPDK 1440 HYIYVVRILWEGQIEPSFVF RTFVEFQELH NKLSIIPPLW KLPGPPNRNV LGRTHIKDVA 1500 AERKIELNSYLQSLMNASTD VAECDLVCTP PHPLLRDEKA EGIARSADAG SFSPTPGQIG 1560 GAVKLSISYRNGTLFIMVMH IKDLVTEDGA DPNPYVKTYL LPDNNKTSKR KTKISRKTRN 1620 PTFNEMLVYSGYSKETLRQR ELQLSVLSAE SLRENFFLGG VTLPLKDFNL SKETVKWYQL 1680 TAATYL SeqID NO: 31 DNA sequence Nucleic Acid Accession #: CAT cluster1          11         21         31         41         51|          |          |          |          |          | TTTTTTTTAGAGACTAAACC ATAGCAAGGA GTTTGTGATC ACTGTATAGC GCTGAGTGAA 60 ACCTCAAAATACATTCTGGA ATTTGTAAGG GATGCTTTCG TCGACTTTTT TTTTTTTTTT 120 TTGGTATTTTCACTGTCAAT TATGCCTCGT ATTATTTATT TATTTGCCAA AATACGACTG 180 TATGAAAAAAAGCTACCTCA TAGAGCTCAT GACACATAAT AGGTATTCAC TGAGCATTTG 240 GTGATTTGTTAAGCACTCAC ATCAATAAAA TATTTCAGCT CAACAGGCAC ACTAGGGGCC 300 AGATGAGCACTGACTTTCCC CATTGAGGAG TCTCGATTAC CTCATGTCTC ACTTCAAACA 360 ATTTATTTTTCTTGTATGCA TAGCTGGGTT CAAGAGTTCT TTCTTGTTTT GTCGGATATA 420 TTCTTTTTCTTTTGTTTTTG TAGGTCCTAT AATACAGTAA AGACATCAAA TAGACC Seq ID NO: 32 DNAsequence Nucleic Acid Accession #: CAT cluster1          11         21         31         41         51|          |          |          |          |          | CAGTCAGATTTTTTTTTTGC TTAACTAAGA CAAAGTGAAT AATTCACTGT GAGCCAAATT 60 CTTTCTTGATTCCTCTTTTT GGAGCAGTCC ATCTTTATGG GAAAACCAGC CTAGAATGGT 120 GATTTCAGTTTCAGGTGATT TCGATAGAAT TGTATTTGGC TCAGAAATGA TAAGACTGGG 180 GCCAAGAAAAATTTTAAACT TTTTTTTTTG TAATCATATT ACTAGTTTGA TTTCATATGA 240 ACTTCCTTTGTTGACTTTCT TTGCCATTAA TTTAAAAGTT CCAGTATCCT CAATATTTGA 300 TGTCTTATATGTACAGAATC CTTTCCAGCT GTAAGTCATC AGCAAGTAAA AAATTTAGTA 360 TGGCAATAGTTTTCATAAGA GGTTTTTTAA AACAGAAAAA TGTTGACATT GCCAGCCTCT 420 GGGTTGCATTTTGGGATATG CTACATTTCA AAGGTATCTT TTAAATCTGA AGGCAAAGAC 480 TTTTTCAACATCTGAATATT CTGATTTACA GAAATTATAA AAAAAAAAGT CGACGCG Seq ID NO: 33 DNAsequence Nucleic Acid Accession #: AK026418.11          11         21         31         41         51|          |          |          |          |          | TTTTAAGATGGAGTTTTCGC TCTTGTTGCC CAGGCTGGAG TGCAGTGGTG CAATCTTGGC 60 TCACTGCAACCTCTGCCCCC CGGGTTCAGG CGATTCTCTC CTCTCAGTCT CTCAAGTAAC 120 TGGGATTACAGGCACACACC ACCACGGCCA GCTAATTATT TTGTATTTTG AGTCGAGAGG 180 AGAATTCACCATATTGGCCT CAGGTAATCC GCCCGCCTCG GCCTCCCAAA GTGTTGGGAT 240 TATGGGCGTGAGCCAGCCAC GGTGCCCGGC CCGTTTTATT GTTTGAAAAA CAAGTACAGG 300 TTGTTATTATCCAAGAATTG TTGATAGAGT ATATACTGTA TTTGAAGTGT AGAACTGAGG 360 CAGAGGCTGATTAATATAAC TAGTTTACAT TTGTTAGCCT TTCACATCTG TGAAGGAATA 420 AAGTACAGACAAAAGTGGAA AACAAACCAG AAAAAAAAAA ATTGTGAAGC ACAGAGCTGC 480 TTAAAAGAGTGGTGTCACAT TAAAAGAAAA AAGTCACAGA AATAAGTCAG TATTTTGTTT 540 AGAGACTAGAACTCCAACTG CTAGCCAACT GCCTAGAATA TAGTAAATAT TTTCTAGTTT 600 CTTAAATGACTAGTAATATT CCTACATTAT GTGATGGCAT TTCCCAAACT GTTTAATTAG 660 ATGTTAGATTTGTAGCCAAA TATGTCTAGG AAATGCTTAA ACAATATAAA ACAGTTTTAA 720 TGATTGGCTTTTTAGAACGT TATATATTAG TGTGCTTTAT GCATATCCAA GAGGTGAGTG 780 AGGTATTTGGGGTTTTTCAG ACTTACTTGA TTACAGATCT GGAGTATCTC AAAACAGTTG 840 TTTTGTGGAAAACACTTTGG CAAACTCTGA GTCTTAGTCA TTAAAAATAG TTTTTGGGTA 900 AACAACAGTGTAATAGAAAT GGAAATTACT GATTCACATT GAGCCATGAA GAATTTATTT 960 TCAGCGATTTTTATAGAAGT TGCTTTATGA CAAAGAAAGC TTTGGTTAAC TGGCATTTGG 1020 CATTTCACACCCCTAAATTT TCTACATGAG GATTTATTTC TCTGGTTCTC TCACTTTCTC 1080 ACTCAGTTATACTGAATTCA TTTATGATGA GCGCTCTCAA CCATTCTTAT TCATCAAAGC 1140 TGAAGTTGGCAGAGCCCTCT CTGGTACCTG ATTAGAAGTC CGTCTTCCGT CTCATAGGGA 1200 AGTGTTAGAGATGGATAATG TTTCTGTGTA GCAGAAGTAG TCATTATGTC CCCTTAAATT 1260 CGGTCACTTTGACTGCAGTA GAGCTTCTTA GTGAGCAGTC TGTGATGGAG TATACTTTCG 1320 GAGAAGCTCATGGTGGGGGA AACCTGGAAT TTATCTAAAT ATTTCATTTC TTTGATAAAT 1380 TACATTAAAAAATTAATAAG AGTATCTATT TGGTGAAATC ATTTTCCTCC ACGTGACCAA 1440 ATGAGAAATTTAGTGAAAGA TTTAAAATCA TTTTTCAGAC TTTTTCCACA TTAGTTGGGA 1500 AGCAAACCCCTTTTTTAAGG CAATGTCAGT TATTAAGCTT TAGGGAACCA CATGCCACTT 1560 TAGGTAACACATGATTGGAG AGATTGAAGA GTGAAGTCCC TGCTTTAAAG TGTACTCCTG 1620 TGGACACAGTAATGCATATA TTTAAAATGG TTCATGTTAA GAGTAGGTAT ATTTCTATCT 1680 AAATACTCTGTAGCTTTTGT GATTCAGGGA AATGAGTGGA GCCTCACAGG CACAAGAATC 1740 TAGTAAATTCTAGGTTTCTT GTGTGGAACT CAGTGGGCAA AATCTTAACT GAGTGAATTC 1800 TTGATTATTGGTATCACATT TATTAGTCTG TATGTATCTG TGTCATCGAT CTCCTTAAGA 1860 AGAGACTCGTAGATATTGAC TGGGAGACCC AAGCTGAATG CTAAAATCTG CTCCATGGAT 1920 ATAAGCTGATGCAGTCATCA TTTCACATTA AAATGTACCA CAGCTATATA TGCCGCAAAA 1980 AAAAAAAAAAAAAA Seq ID NO: 34 DNA sequence Nucleic Acid Accession #: CAT cluster1          11         21         31         41         51|          |          |          |          |          | CTACTACTAAATTCGCGGCC GCGTCGACTT TTTTTTTTTT TTGTCTTATG TCTCTAATCT 60 GCACTGTTCAGCTCTTTTAG GCACTGCAAA GTTGTCTTGA ATTAGGAAAG AGGTGCTAGA 120 ATGTGGGCGTGGGTGTTGAC CTACATCTGA ACAATTTACA TATGATTCAC CACAATTAAA 180 CAATTTGGTTTGAAATAGCT ATAATTAAGT TATTATCAGA GAAGTATTTA CTAGTCTAGA 240 AATTCTAAATTTATCTTCAC ATACACCCTA ACTGAGAAAA GGGCCACATT TTCTGCACTC 300 TATTAAGTAAAGCAAATGCT GAACTAAATG CCTCCATGTT AACATTTATA TTGTTAAGTT 360 ACTGACAGCATATTCTATGA ATGATTACGT TAGTCGTTTC TTTAAAAATT ATAGGTTTGA 420 AATAGCAAGAAAAATATGAA ATGATGGTAG ACAAAAAAGA GTTTCAGTTT CTAACTTCTA 480 ACTATATATATACACACACA CATGCACACA GAATTGCCTT CCCGGATGTA TAGAAATTAT 540 ATACAGCCATGTCCAGGCNC GATGGAAATT ATGGGGGAAT ATCCAANTTA GGATACNCGT 600 GCCGAATCGCCGGGTNTAAA TAATACNGGT CNATCCACCA TCCTGGTTTA Seq ID NO: 35 DNA sequenceNucleic Acid Accession #: NM_018490.1 Coding sequence: 445..33001          11         21         31         41         51|          |          |          |          |          | CCGCGGCTGGGAGACAGCGA GCCAGAGTCT GGGTGTTTGT GCGAGAGCCA CGGCGGGGGC 60 TGGGGCGAGTGGCCGGCATG GCTGAAGGCT GCGCTCTGCA ACCTTGAAGA GCCGCTGCAT 120 TGAGAGGCCAGGGACAGGGA GACCGGTGCG ATGGCAGAGC GCGGCCCCCG CCGCTGCGCC 180 GGGCCGGCCCGGCTGGCCTG AGCCGCCGGA GGAGCGGGGC TGCCTCTGCG CGTCCATGGA 240 GCAGCGGGAAGGGCGAAACT CCGGAGCGCC GCGTCCCTGC GCCGCTGCGG CGGACTGCTG 300 AAGGGGCCGAGCCCGCGCGG ACCGCCGAGG AAGAGACCCC CGCTCCAGCC CGCAGGCCGG 360 CTGCCCGGGGGCGGCGGGGG ACATCGGAGG GCAGCGGAGC GAGCAGCGCC GCGGGAGAGG 420 CCGGCGCGGGAGGCGGCCGC AGCAATGCCG GGCCCGCTAG GGCTGCTCTG CTTCCTCGGC 480 CTGGGGCTGCTCGGCTCGGC CGGGCCCAGC GGCGCGGCGC CGCCTCTCTG CGCGGCGCCC 540 TGCAGCTGCGACGGCGACCG TCGGGTGGAC TGCTCCGGGA AGGGGCTGAC GGCCGTGCCC 600 GAGGGGCTCAGCGCCTTCAC CCAAGCGCTG GATATCAGTA TGAACAACAT TACTCAGTTG 660 CCAGAAGATGCATTTAAGAA CTTTCCTTTT CTAGAAGAGC TACAATTGGC GGGCAACGAC 720 CTTTCTTTTATCCACCCAAA GGCCTTGTCT GGGTTGAAAG AACTCAAAGT TCTAACGCTC 780 CAGAATAATCAGTTGAAAAC AGTACCCAGT GAAGCCATTC GAGGGCTGAG TGCTTTGCAG 840 TCTTTGCGTTTAGATGCCAA CCATATTACC TCAGTCCCCG AGGACAGTTT TGAAGGACTT 900 GTTCAGTTACGGCATCTGTG GCTGGATGAC AACAGCTTGA CGGAGGTGCC TGTGCACCCC 960 CTCAGGAACTTGCCCACCCT ACAGGCGCTG ACCCTGGCTC TCAACAAGAT CTCAAGCATC 1020 CCTGACTTTGCATTTACCAA CCTTTCAAGC CTGGTAGTTC TGCATCTTCA TAACAATAAA 1080 ATTAGAGGCCTGAGTCAACA CTGTTTTGAT GGACTAGATA ACCTGGAGAC CTTAGACTTG 1140 AGTTATAATAACTTGGGGGA ATTTCCTCAG GCTATTAAAG CCCGTCCTAG CCTTAAAGAG 1200 CTAGGATTTCATAGTAATTC TATTTCTGTT ATCCCTGATG GAGCATTTGA TGGTAATCCA 1260 CTCTTAAGAACTATACATTT GTATGATAAT CCTCTGTCTT TTGTGGGGAA CTCAGCATCT 1320 CACAATTTATCTGATCTTCA TTCCCTAGTC ATTCGTGGTG CAAGCATGGT GCAGCAGTTC 1380 CCCAATCTTACAGGAACTGT CCACCTGGAA AGTCTGACTT TGACAGGTAC AAAGATAAGC 1440 AGCATACCTAATAATTTGTG TCAAGAACAA AAGATGCTTA GGACTTTGGA CTTGTCTTAC 1500 AATAATATAAGAGACCTTCC AAGTTTTAAT GGTTGCCATG CTCTGGAAGA AATTTCTTTA 1560 CAGCGTAATCAAATCTACCA AATAAAGGAA GGCACCTTTC AAGGCCTGAT ATCTCTAAGG 1620 ATTCTAGATCTGAGTAGAAA CCTGATACAT GAAATTCACA GTAGAGCTTT TGCCACACTT 1680 GGGCCAATAACTAACCTAGA TGTAAGTTTC AATGAATTAA CTTCCTTTCC TACGGAAGGC 1740 CCGAATGGGCTAAATCAACT GAAACTTGTG GGCAACTTCA AGCTGAAAGA AGCCTTAGCA 1800 GCAAAAGACTTTGTTAACCT CAGGTCTTTA TCGGTACCAT ATGCTTATCA GTGCTGTGCA 1860 TTTTGGGGTTGTGACTCTTA TGCAAATTTA AACACAGAAG ATAACAGCCT CCAGGACCAC 1920 AGTGTGGCACAGGAGAAAGG TACTGCTGAT GCAGCAAATG TCACAAGCAC TCTTGAAAAT 1980 GAAGAACATAGTCAAATAAT TATCCATTGT ACACCTTCAA CAGGTGCTTT TAAGCCCTGT 2040 GAATATTTACTGGGAAGCTG GATGATTCGT CTTACTGTGT GGTTCATTTT CTTGGTTGCA 2100 TTATTTTTCAACCTGCTTGT TATTTTAACA ACATTTGCAT CTTGTACATC ACTGCCTTCG 2160 TCCAAATTGTTTATAGGCTT GATTTCTGTG TCTAACTTAT TCATGGGAAT CTATACTGGC 2220 ATCCTAACTTTTCTTGATGC TGTGTCCTGG GGCAGATTCG CTGAATTTGG CATTTGGTGG 2280 GAAACTGGCAGTGGCTGCAA AGTAGCTGGG TTTCTTGCAG TTTTCTCCTC AGAAAGTGCC 2340 ATATTTTTATTAATGCTAGC AACTGTCGAA AGAAGCTTAT CTGCAAAAGA TATAATGAAA 2400 AATGGGAAGAGCAATCATCT CAAACAGTTC CGGGTTGCTG CCCTTTCGGC TTTCCTAGGT 2460 GCTACAGTAGCAGGCTGTTT TCCCCTTTTC CATAGAGGGG AATATTCTGC ATCACCCCTT 2520 TGTTTGCCATTTCCTACAGG TGAAACGCCA TCATTAGGAT TCACTGTAAC GTTAGTGCTA 2580 TTAAACTCACTAGCATTTTT ATTAATGGCC GTTATCTACA CTAAGCTATA CTGCAACTTG 2640 GAAAAAGAGGACCTCTCAGA AAACTCACAA TCTAGCATGA TTAAGCATGT CGCTTGGCTA 2700 ATCTTCACCAATTGCATCTT TTTCTGCCCT GTGGCGTTTT TTTCATTTGC TTTTCCATTG 2820 CCTGCTTGCCTGAATCCAGT CCTGTATGTT TTCTTCAACC CAAAGTTTAA AGAAGACTGG 2880 AAGTTACTGAAGCGACGTGT TACCAAGAAA AGTGGATCAG TTTCAGTTTC CATCAGTAGC 2940 CAAGGTGGTTGTCTGGAACA GGATTTCTAC TACGACTGTG GCATGTACTC ACATTTGCAG 3000 GGCAACCTGACTGTTTGCGA CTGCTGCGAA TCGTTTCTTT TAACAAAGCC AGTATCATGC 3060 AAACACTTGATAAAATCACA CAGCTGTCCT GCATTGGCAG TGGCTTCTTG CCAAAGACCT 3120 GAGGGCTACTGGTCCGACTG TGGCACACAG TCGGCCCACT CTGATTATGC AGATGAAGAA 3180 GATTCCTTTGTCTCAGACAG TTCTGACCAG GTGCAGGCCT GTGGACGAGC CTGCTTCTAC 3240 CAGAGTAGAGGATTCCCTTT GGTGCGCTAT GCTTACAATC TACCAAGAGT TAAAGACTGA 3300 ACTACTGTGTGTGTAACCGT TTCCCCCGTC AACCAAAATC AGTGTTTATA GAGTGAACCC 3360 TATTCTCATCTTTCATCTGG GAAGCACTTC TGTAATCACT GCCTGGTGTC ACTTAGAAGA 3420 AGGAGAGGTGGCAGTTTATT TCTCAAACCA GTCATTTTCA AAGAACAGGT GCCTAAATTA 3480 TAAATTGGTGAAAAATGCAA TGTCCAAGCA ATGTATGATC TGTTTGAAAC AAATATATGA 3540 CTTGAAAAGGATCTTAGGTG TAGTAGAGCA ATATAATGTT AGTTTTTTCT GATCCATAAG 3600 AAGCAAATTTATACCTATTT GTGTATTAAG CACAAGATAA AGAACAGCTG TTAATATTTT 3660 TTAAAAATCTATTTTAAAAT GTGATTTTCT ATAACTGAAG AAAATATCTT GCTAATTTTA 3720 CCTAATGTTTCATCCTTAAT CTCAGGACAA CTTACTGCAG GGCCAAAAAA GGGACTGTCC 3780 CAGCTAGAACTGTGAGAGTA TACATAGGCA TTACTTTATT ATGTTTTCAC TTGCCATCCT 3840 TGACATAAGAGAACTATAAA TTTTGTTTAA GCAATTTATA AATCTAAAAC CTGAAGATGT 3900 TTTTAAAACAATATTAACAG CTGTTAGGTT AAAAAAATAG CTGGACATTT GTTTTCAGTC 3960 ATTATACATTGCTTTGGTCC AATCAGTAAT TTTTTCTTAA GTGTTTTGTG ATTACACTAC 4020 TAGAAAAAAAGTAAAAGGCT AATTGCTGTG TGGGTTTAGT CGATTTGGCT AAACTACTAA 4080 CTAATGTGGGGGTTTAATAG TATCTGAGGG ATTTGGTGGC TTCATGTAAT GTTCTCATTA 4140 ATGAATACTTCCTAATATCG TTGGCTCTAC TAATATTTTC CAATTTGCTG GGATGTCACC 4200 TAGCAATAGCTTGGATTATA TAGAAAGTAA ACTGTGGTCA ATACTTGCAT TTAATTAGAC 4260 GAAACGGGGAGTAATTATGA CACGAAGTAC TTATGTTTAT TTCTTAGTGA GCTGGATTAT 4320 CTTGAACCTGTGCTATTAAA TGGAAATTTC CATACATCTT CCCCATACTA TTTTTTATAA 4380 AAGAGCCTATTCAATAGCTC AGAGGTTGAA CTCTGGTTAA ACAAGATAAT ATGTTATTAA 4440 TAAAAATAGAAGAAGAAAGA ATAAAGCTTA GTCCTGTGTC TTTAAAAATT AAAAATTTTA 4500 CTTGATTCCCATCTATGGGC TTTAGACCTA TTACTGGGTG GAGTCTTAAA GTTATAATTG 4560 TTCAATATGTTTTTTGAACA GTGTGCTAAA TCAATAGCAA ACCCACTGCC ATATTAGTTA 4620 TTCTGAATATACTAAAAAAA TCCAGCTAGA TTGCAGTTTA ATAATTAAAC TGTACATACT 4680 GTGCATATAATGAATTTTTA TCTTATGTAA ATTATTTTTA GAACACAAGT TGGGAAATGT 4740 GGCTTCTGTTCATTTCGTTT AATTAAAGCT ACCTCCTAAA CATAAGTGGC TGCCAGTAGC 4800 AGACTGTTAAATTGTGGTTT ATATACTTTT TGCATTGTAA ATAGTCTTTG TTGTACATTG 4860 TCAGTGTAATAAAAACAGAA TCTTTGTATA TCAAAATCAT GTAGTTTGTA TAAAATGTGG 4920 GAAGGATTTATTTACAGTGT GTTGTAATTT TGTAAGGCCA ACTATTTACA AGTTTTAAAA 4980 ATTGCTATCATGTATATTTA CACATCTGAT AAATATTAAA TCATAACTTG GTAAGAAACT 5040 CCTAATTAAAAGGTTTTTTC CAAAATTCAG GTTATTGAAA ATTTTTCATT TTATTCATTT 5100 AAAAACTAGAATAACAGATA TATAAAAGTG TTAATCTTTG TGCTATATGG TATGAAATAC 5160 AATATTGTACTCAGTGTTTT GAATTATTAA AGTTTCTAGA AAGCAAAAAA A Seq ID NO: 36 Proteinsequence Protein Accession #: NP_060960.11          11         21         31         41         51|          |          |          |          |          | MPGPLGLLCGLALGLLGSAG PSGAAPPLCA APCSCDGDRR VDCSGKGLTA VPEGLSAFTQ 60 ALDISMNNITQLPEDAFKNF PFLEELQLAG NDLSFIGPKA LSGLKELKVL TLQNNQLKTV 120 PSEAIRGLSALQSLRLDANH ITSVPEDSFE GLVQLRHLWL DDNSLTEVPV HPLSNLPTLQ 180 ALTLALNKISSIPDFAFTNL SSLVVLHLHN NKIRGLSQHC FDGLDNLETL DLSYNNLGEF 240 PQAIKARPSLKELGPHSNSI SVIPDGAFDG NPLLRTIGLY DNPLSFVGNS ASHNLSDLHS 300 LVIRGASMVQQFPNLTGTVH LESLTLTGTK ISSIPNNLCQ EQKMLRTLDL SYNNIRDLPS 360 FNGCHALEEISLQRNQIYQI KEGTFQGLIS LRILDLSRNL IHEIHSRAFA TLGPITNLDV 420 SFNELTSFPTEGPNGLNQLK LVGNFKLKEA LAAKDFVNLR SLSVPYAYQC CAFWGCDSYA 480 NLNTEDNSLQDHSVAQEKGT ADAANVTSTL ENEEHSQIII HCTPSTGAFK PCEYLLGSWM 540 IRLTVWFIFLVALFFNLLVI LTTFASCTSL PSSKLFIGLI SVSNLFMGIY TGILTFLDAV 600 SWGRFAEFGIWWETGSGCKV AGFLAVFSSE SAIFLLMLAT VERSLSAKDI MKNGKSNHLK 660 QFRVAALSAFLGATVAGCFP LFHRGEYSAS PLCLPFPTGE TPSLGFTVTL VLLNSLAFLL 720 MAVIYTKLYCNLEKEDLSEN SQSSMIKHVA WLIFTNCIFF CPVAFFSFAP LITAISISPE 780 IMKSVTLIFFPLPACLNPVL YVFFNPKFKE DWKLLDRRVT KKSGSVSVSI SSQGGCLEQD 840 FYYDCGMYSHLQGNLTVCDC CESFLLTKPV SCKHLIKSHS CPALAVASCQ RPEGYWSDCG 900 TQSAHSDYADEEDSFVSDSS DQVQACGRAC FYQSRGFPLV RYAYNLPRVK D Seq ID NO:37 DNA sequenceNucleic Acid Accession #: AF144648.1 Coding sequence: 1..18841          11         21         31         41         51|          |          |          |          |          | ATGCTGCGAGCCGCAGTGAT CCTGCTGCTC ATCAGGACCT GGCTCGCGGA GGGCAACTAC 60 CCCAGTCCCATCCCGAAATT CCACTTCGAG TTCTCCTCTG CTGTGCCCGA AGTCGTCCTG 120 AACCTCTTCAACTGCAAAAA TTGTGCAAAT GAAGCTGTGG TTCAAAAGAT TTTGGACAGG 180 GTGCTGTCAAGATACGATGT CCGCCTGAGA CCGAATTTTG GAGGTGCCCC TGTGCCTGTG 240 AGAATATCTATTTATGTCAC GAGCATTGAA CAGATCTCAG AAATGAATAT GGACTACACG 300 ATCACGATGTTTTTTCATCA GACTTGGAAA GATTCACGCT TAGCATACTA TGAGACCACC 360 CTGAACTTGACCCTGGACTA TCGGATGCAT GAGAAGTTGT GGGTCCCTGA CTGCTACTTT 420 TTGAACAGCAAGGATGCTTT CGTGCATGAT GTGACTGTGG AGAATCGCGT GTTTCAGCTT 480 CACCCAGATGGAACGGTGCG GTACGGCATC CGACTCACCA CTACAGCAGC TTGTTCCCTG 540 GATCTGCATAAATTCCCTAT GGACAAGCAG GCCTGCAACC TGGTGGTAGA GAGCTATGGT 600 TACACGGTTGAAGACATCAT ATTATTCTGG GATGACAATG GGAACGCCAT CCACATGACT 660 GAGGAGCTGCATATCCCTCA GTTCACTTTC CTGGGAAGGA CGATTACTAG CAAGGAGGTG 720 TATTTCTACACAGGTTCCTA CATACGCCTG ATACTGAAGT TCCAGGTTCA GAGGGAAGTT 780 AACAGCTACCTTGTGCAAGT CTACTGGCCT ACTGTCCTCA CCACTATTAC CTCTTGGATA 840 TCGTTTTGGATGAACTATGA TTCCTCTGCA GCCAGGGTGA CAATTGGCTT AACTTCAATG 900 CTCATCCTGACCACCATCGA CTCACATCTG CGGGATAAGC TCCCCAACAT TTCCTGTATC 960 AAGGCCATTGATATCTATAT CCTCGTGTGC TTGTTCTTTG TGTTCCTGTC CTTGCTGGAG 1020 TATGTCTACATCAACTATCT TTTCTACAGT CGAGGACCTC GGCGCCAGCC TAGGCGACAC 1080 AGGAGACCCCGAAGAGTCAT TGCCCGCTAC CGCTACCAGC AAGTGGTGGT AGGAAACGTG 1140 CAGGATGGCCTGATTAACGT GGAAGACGGA GTCAGCTCTC TCCCCATCAC CCCAGCGCAG 1200 GCCCCCCTGGCAAGCCCGGA AAGCCTCGGT TCTTTGACGT CCACCTCCGA GCAGGCCCAG 1260 CTGGCCACCTCGGAAAGCCT CAGCCCACTC ACTTCTCTCT CAGGCCAGGC CCCCCTGGCC 1320 ACTGGAGAAAGCCTGAGCGA TCTCCCCTCC ACCTCAGAGC AGGCCCGGCA CAGCTATGGT 1380 GTTCGCTTTAATGGTTTCCA GGCTGATGAC AGTATTTTTC CTACCGAAAT CCGCAACCGT 1440 GTCGAAGCCCATGGCCATGG TGTTACCCAT GACCATGAAG ATTCCAATGA GAGCTTGAGC 1500 TCGGATGAGCGCCATGGCCA TGGCCCCAGT GGGAAGCCCA TGCTTCACCA TGGCGAGAAG 1560 GGTGTGCAAGAAGCAGGCTG GGACCTTGAT GACAACAATG ACAAGAGCGA CTGCCTTGCC 1620 ATTAAGGAGCAATTCAAGTG TGATACTAAC AGTACCTGGG GCCTTAATGA TGATGAGCTC 1680 ATGGCCCATGGCCAAGAGAA GGACAGTAGC TCAGAGTCTG AGGATAGTTG CCCCCCAAGC 1740 CCTGGGTGCTCCTTCACTGA AGGGTTCTCC TTCGATCTCT TTAATCCTGA CTACGTCCCA 1800 AAGGTCGACAAGTGGTCCCG GTTCCTCTTC CCTCTGGCCT TTGGGTTGTT CAACATTGTT 1860 TACTGGGTATACCATATGTA TTAG Seq ID NO: 38 Protein sequence Protein Accession #:AAD51172.1 1          11         21         31         41         51|          |          |          |          |          | MLRAAVILLLIRTWLAEGNY PSPIPKFHFE FSSAVPEVVL NLFNCKNCAN EAVVQKILDR 60 VLSRYDVRLRPNFGGAPVPV RISIYVTSIE QISEMNMDYT ITMFFHQTWK DSRLAYYETT 120 LNLTLDYRMNEKLWVPDCYF LNSKDAFVHD VTVENRVFQL HPDGTVRYGI RLTTTAACSL 180 DLHKFPMDKQACNLVVESYG YTVEDIILFW DDNGNAIHMT EELHIPQFTF LGRTITSKEV 240 YFYTGSYIRLILKFQVQREV NSYLVQVYWP TYLTTITSWI SFWMNYDSSA ARVTIGLTSM 300 LILTTIDSHLRDKLPNISCI KAIDIYILVC LFFVFLSLLE YVYINYLFYS RGPRRQPRRH 360 RRPRRVIARYRYQQVVVGNV QDGLINVEDG VSSLPITPAQ APLASPESLG SLTSTSEQAQ 420 LATSESLSPLTSLSGQAPLA TGESLSDLPS TSEQARHSYG VRFNGFQADD SIFPTEIRNR 480 VEAHGHGVTHDHEDSNESLS SDERHGHGPS GKPMLHHGEK GVQEAGWDLD DNNDKSDCLA 540 IKEQFKCDTNSTWGLNDDEL MAHGQEKDSS SESEDSCPPS PGCSFTEGFS FDLFNPDYVP 600 KVDKWSRFLFPLAFGLFNIV YWVYHMY Seq ID NO: 39 DNA sequence Nucleic Acid Accession #:U47334.1 Coding sequence: 1..3311          11         21         31         41         51|          |          |          |          |          | CAAAAATTGTGCAAATGAAG CTGTGGTTCA AAAGATTTTG GACAGGGTGC TGTCAAGATA 60 CGATGTCCGCCTGAGACCGA ATTTTGGANN NATGCTTGCT ACTAACAGTA CCCGGGGCCT 120 TAATGAAGATGAGCTCATGG CCCATGGCCA AGAGAAGGAC AGTAGCTCAG AGTCTGAGGA 180 TAGTTGCCCCCCAAGCCCTG GGTGCTCCTT CACTGAAGGG TTCTCCTTCG ATCTCCTTAA 240 TCCTGACTACGTCCCAAAGG TCGACAAGTG GTCCCGGTTC CTCTTCCCTC TGGCCTTTGG 300 GTTGTTCAACATTGTAGCGG CCGAACGATG C Seq ID NO: 40 Protein sequence Protein Accession#: AAC50559.1 1          11         21         31         41         51|          |          |          |          |          | KNCANEAVVQKILDRVLSRY DVRLRPNFGX MLATNSTRGL NEDELMAHGQ EKDSSSESED 60 SCPPSPGCSFTEGFSFDLLN PDYVPKVDKW SRFLFPLAFG LFNIVAAERC Seq ID NO: 41 DNA sequenceNucleic Acid Accession #: NM_020974 Coding sequence: 81..30801          11         21         31         41         51|          |          |          |          |          | GGCGTCCGCGCACACCTCCC CGCGCCGCCG CCGCCACCGC CCGCACTCCG CCGCCTCTGC 60 CCGCAACCGCTGAGCCATCC ATGGGGGTCG CGGGCCGCAA CCGTCCCGGG GCGGCCTGGG 120 CGGTGCTGCTGCTGCTGCTG CTGCTGCCGC CACTGCTGCT GCTGGCGGGG GCCGTCCCGC 180 CGGGTCGGGGCCGTGCCGCG GGGCCGCAGG AGGATGTAGA TGAGTGTGCC CAAGGGCTAG 240 ATGACTGCCATGCCGACGCC CTGTGTCAGA ACACACCCAC CTCCTACAAG TGCTCCTGCA 300 AGCCTGGCTACCAAGGGGAA GGCAGGCAGT GTGAGGACAT CGATGAATGT GGAAATGAGC 360 TCAATGGAGGCTGTGTCCAT GACTGTTTGA ATATTCCAGG CAATTATCGT TGCACTTGTT 420 TTGATGGCTTCATGTTGGCT CATGACGGTC ATAATTGTCT TGATGTGGAC GAGTGCCTGG 480 AGAACAATGGCGGCTGCCAG CATACCTGTG TCAACGTCAT GGGGAGCTAT GAGTGCTGCT 540 GCAAGGAGGGGTTTTTCCTG AGTGACAATC AGCACACCTG CATTCACCGC TCGGAAGAGG 600 GCCTGAGCTGCATGAATAAG GATCACGGCT GTAGTCACAT CTGCAAGGAG GCCCCAAGGG 660 GCAGCGTCGCCTGTGAGTGC AGGCCTGGTT TTGAGCTGGC CAAGAACCAG AGAGACTGCA 720 TCTTGACCTGTAACCATGGG AACGGTGGGT GCCAGCACTC CTGTGACGAT ACAGCCGATG 780 GCCCAGAGTGCAGCTGCCAT CCACAGTACA AGATGCACAC AGATGGGAGG AGCTGCCTTG 840 AGCGAGAGGACACTGTCCTG GAGGTGACAG AGAGCAACAC CACATCAGTG GTGGATGGGG 900 ATAAACGGGTGAAACGGCGG CTGCTCATGG AAACGTGTGC TGTCAACAAT GGAGGCTGTG 960 ACCGCACCTGTAAGGATACT TCGACAGGTG TCCACTGCAG TTGTCCTGTT GGATTCACTC 1020 TCCAGTTGGATGGGAAGACA TGTAAAGATA TTGATGAGTG CCAGACCCGC AATGGAGGTT 1080 GTGATCATTTCTGCAAAAAC ATCGTGGGCA GTTTTGACTG CGGCTGCAAG AAAGGATTTA 1140 AATTATTAACAGATGAGAAG TCTTGCCAAG ATGTGGATGA GTGCTCTTTG GATAGGACCT 1200 GTGACCACAGCTGCATCAAC CACCCTGGCA CATTTGCTTG TGCTTGCAAC CGAGGGTACA 1260 CCCTGTATGGCTTCACCCAC TGTGGAGACA CCAATGAGTG CAGCATCAAC AACGGAGGCT 1320 GTCAGCAGGTCTGTGTGAAC ACAGTGGGCA GCTATGAATG CCAGTGCCAC CCTGGGTACA 1380 AGCTCCACTGGAATAAAAAA GACTGTGTGG AAGTGAAGGG GCTCCTGCCC ACAAGTGTGT 1440 CACCCCGTGTGTCCCTGCAC TGCGGTAAGA GTGGTGGAGG AGACGGGTGC TTCCTCAGAT 1500 GTCACTCTGGCATTCACCTC TCTTCAGATG TCACCACCAT CAGGACAAGT GTAACCTTTA 1560 AGCTAAATGAAGGCAAGTGT AGTTTGAAAA ATGCTGAGCT GTTTCCCGAG GGTCTGCGAC 1620 CAGCACTACCAGAGAAGCAC AGCTCAGTAA AAGAGAGCTT CCGCTACGTA AACCTTACAT 1680 GCAGCTCTGGCAAGCAAGTC CCAGGAGCCC CTGGCCGACC AAGCACCCCT AAGGAAATGT 1740 TTATCACTGTTGAGTTTGAG CTTGAAACTA ACCAAAAGGA GGTGACAGCT TCTTGTGACC 1800 TGAGCTGCATCGTAAAGCGA ACCGAGAAGC GGCTCCGTAA AGCCATCCGC ACGCTCAGAA 1860 AGGCCGTCCACAGGGAGCAG TTTCACCTCC AGCTGTCAGG CATGAACCTC GACGTGGCTA 1920 AAAAGCCTCCCAGAACATCT GAACGCCAGG CAGAGTCCTG TGGAGTGGGC CAGGGTCATG 1980 CAGAAAACCAATGTGTCAGT TGCAGGGCTG GGACCTATTA TGATGGAGCA CGAGAACGCT 2040 GCATTTTATGTCCAAATGGA ACCTTCCAAA ATGAGGAAGG ACAAATGACT TGTGAACCAT 2100 GCCCAAGACCAGGAAATTCT GGGGCCCTGA AGACCCCAGA AGCTTGGAAT ATGTCTGAAT 2160 GTGGAGGTCTGTGTCAACCT GGTGAATATT CTGCAGATGG CTTTGCACCT TGCCAGCTCT 2220 GTGCCCTGGGCACGTTCCAG CCTGAAGCTG GTCGAACTTC CTGCTTCCCC TGTGGAGGAG 2280 GCCTTGCCACCAAACATCAG GGAGCTACTT CCTTTCAGGA CTGTGAAACC AGAGTTCAAT 2340 GTTCACCTGGACATTTCTAC AACACCACCA CTCACCGATG TATTCGTTGC CCAGTGGGAA 2400 CATACCAGCCTGAATTTGGA AAAAATAATT GTGTTTCTTG CCCAGGAAAT ACTACGACTG 2460 ACTTTGATGGCTCCACAAAC ATAACCCAGT GTAAAAACAG AAGATGTGGA GGGGAGCTGG 2520 GAGATTTCACTGGGTACATT GAATCCCCAA ACTACCCAGG CAATTACCCA GCCAACACCG 2580 AGTGTACGTGGACCATCAAC CCACCCCCCA AGCGCCGCAT CCTGATCGTG GTCCCTGAGA 2640 TCTTCCTGCCCATAGAGGAC GACTGTGGGG ACTATCTGGT GATGCGGAAA ACCTCTTCAT 2700 CCAATTCTGTGACAACATAT GAAACCTGCC AGACCTACGA ACGCCCCATC GCCTTCACCT 2760 CCAGGTCAAAGAAGCTGTGG ATTCAGTTCA AGTCCAATGA AGGGAACAGC GCTAGAGGGT 2820 TCCAGGTCCCATACGTGACA TATGATGAGG ACTACCAGGA ACTCATTGAA GACATAGTTC 2880 GAGATGGCAGGCTCTATGCA TCTGAGAACC ATCAGGAAAT ACTTAAGGAT AAGAAACTTA 2940 TCAAGGCTCTGTTTGATGTC CTGGCCCATC CCCAGAACTA TTTCAAGTAC ACAGCCCAGG 3000 AGTCCCGAGAGATGTTTCCA AGATCGTTCA TCCGATTGCT ACGTTCCAAA GTGTCCAGGT 3060 TTTTGAGACCTTACAAATGA CTCAGCCCAC GTGCCACTCA ATACAAATGT TCTGCTATAG 3120 GGTTGGTGGGACAGAGCTGT CTTCCTTCTG CATGTCAGCA CAGTCGGGTA TTGCTGCCTC 3180 CCGTATCAGTGACTCATTAG AGTTCAATTT TTATAGATAA TACAGATATT TTGGTAAATT 3240 GAACTTGGTTTTTCTTTCCC AGCATCGTGG ATGTAGACTG AGAATGGCTT TGAGTGGCAT 3300 CAGCTTCTCACTGCTGTGGG CGGATGTCTT GGATAGATCA CGGGCTGGCT GAGCTGGACT 3360 TTGGTCAGCCTAGGTGAGAC TCACCTGTCC TTCTGGGGTC TTACTCCTCC TCAAGGAGTC 3420 TGTAGTGGAAAGGAGGCCAC AGAATAAGCT GCTTATTCTG AAACTTCAGC TTCCTCTAGC 3480 CCGGCCCTCTCTAAGGGAGC CCTCTGCACT CGTGTGCAGG CTCTGACCAG GCAGAACAGG 3540 CAAGAGGGGAGGGAAGGAGA CCCCTGCAGG CTCCCTCCAC CCACCTTGAG ACCTGGGAGG 3600 ACTCAGTTTCTCCACAGCCT TCTCCAGCCT GTGTGATACA AGTTTGATCC CAGGAACTTG 3660 AGTTCTAAGCAGTGCTCGTG AAAAAAAAAA GCAGAAAGAA TTAGAAATAA ATAAAAACTA 3720 AGCACTTCTGGAGACAT Seq ID NO: 42 Protein sequence Protein Accession #: NP_0660251          11         21         31         41         51|          |          |          |          |          | MGVAGRNRPGAAWAVLLLLL LLPPLLLLAG AVPPGRGRAA GPQEDVDECA QGLDDCHADA 60 LCQNTPTSYKCSCKPGYQGE GRQCEDIDEC GNELNGGCVH DCLNIPGNYR CTCFDGFMLA 120 HDGHNCLDVDECLENNGGCQ HTCVNVMGSY ECCCKEGFFL SDNQHTCIHR SEEGLSCMNK 180 DHGCSHICKEAPRGSVACEC RPGFELAKNQ RDCILTCNHG NGGCQHSCDD TADGPECSCH 240 PQYKMHTDGRSCLEREDTVL EVTESNTTSV VDGDKRVKRR LLMETCAVNN GGCDRTCKDT 300 STGVHCSCPVGRTLQLDGKT CKDIDECQTR NGGCDHFCKN IVGSFDCGCK KGFKLLTDEK 360 SCQDVDECSLDRTCDHSCIN HPGTFACACN RGYTLYGFTH CGDTNECSIN NGGCQQVCVN 420 TVGSYECQCHPGYKLHWNKK DCVEVKGLLP TSVSPRVSLH CGKSGGGDGC FLRCHSGIHL 480 SSDVTTIRTSVTFKLNEGKC SLKNAELFPE GLRPALPEKH SSVKESFRYV NLTCSSGKQV 540 PGAPGRPSTPKRMFITVEFE LETNQKEVTA SCDLSCIVKR TEKRLRKAIR TLRKAVHREQ 600 FHLQLSGMNLDVAKKPPRTS ERQAESCGVG QGHAENQCVS CRAGTYYDGA RERCILCPNG 660 TFQNEEGQMTCEPCPRPGNS GALKTPEAWN MSECGGLCQP GEYSADGFAP CQLCALGTFQ 720 PEAGRTSCFPCGGGLATKHQ GATSFQDCET RVQCSPGHFY NTTTHRCIRC PVGTYQPEFG 780 KNNCVSCPGNTTTDFDGSTN ITQCKNRRCG GELGDFTGYI ESPNYPGNYP ANTECTWTIN 840 PPPKRRILIVVPEIFLPIED DCGDYLVMRK TSSSNSVTTY ETCQTYERPI AFTSRSKKLW 900 IQFKSNEGNSARGFQVPYVT YDEDYQELIE DIVRDGRLYA SENHQEILKD KKLIKALFDV 960 LAHPQNYFKYTAQESREMFP RSFIRLLRSK VSERLRPYK Seq ID NO: 43 DNA sequence Nucleic AcidAccession #: CAT cluster1          11         21         31         41         51|          |          |          |          |          | TTTCTTCATTTTATGCTTTT CTCCCCTTTA TATATACTGG GCGGTTTTTC CTTGAGAAAT 60 TTTCCATCTCATTAATTCTC CTGCAGCAAT TCATAACTCT TTGGGGGCAT TCCTTTGTTT 120 TTTGATATGACTACTACCTG ACTGTATATA GTTTCCCTTT TTTTTTTTTC CTCCCAGATT 180 CTCTCCTTTCTACTGGCATC CTTTTCCATT TTACTCAATT TTCCTCAGTT AGGTTGACTT 240 GCTTTTATACCTGTGTGATG CTCCTTGCCA GATATCTAGC AAATGCCCCC AGGATCCAAT 300 CATTTTTTTCCTAAGAAAAC TGAAAAGAAG CATGGCAAAT AACAGAGCTT GGAAAATAGG 360 AAACTTTAAAATACAAAGCC CAGTGAAATC TACTTGGAAG CCAATGCTTA GAGGCAAGAG 420 ACAGTGATTCAAATAGGTGT TGANNNNNNN NNNNNNNNNN NATGATCAGC ATAGCAAAGA 480 TCACTTTCCAACATTGGAAA GTTATGCATA TTCCAATTGA GCTAGCCCTT TTAAACAGCC 540 TTAAAATTGTATAAAAGAGA AGAAATTTAA GATATTGAAA ACTGGTAGAT AATAAAACCT 600 AAATAAAGCTGGTTTTGGAA GAGCAGTGGC CACTGTGATT GACAATGGGG GCACTTACTG 660 TTAAGGGGATTTATAACAGA AGTACTTGAA CAGAATTGTG AAGAGAATAG AATTGTGCAT 720 TCTTTTATCTGCCCAGAACC ACAGCTCCCA TGGGAAATAC TCCACCTCAT TCTACAACCT 780 TCTGGCTGCAACAAAAGCAG TCAAATTAAA ACATAACCCA AAGGGGGTAC CTAACCCAAC 840 TTGAGAAAATCATAGCATNC TCCCTTTGGC TATAACTNTT TCCACATGAA ATACATTCAA 900 ATGCCTT SeqID NO: 44 DNA sequence Nucleic Acid Accession #: CAT cluster1          11         21         31         41         51|          |          |          |          |          | TTTTTTTTTTTTTTTTTGGA TTTTAGTATG CCTTGCAATT TTTTCCCTTT ATTCTGATGC 60 ATGAAGTACCCACTAAAAGT GACTGCTGTT AGTATAGCTT CAGTAATGAG GTGATGAGGT 120 GACAGGGCAGGTGATGCTCT CTTAGTCTCT TTAGGCTACT ATTACAAAAT ACTTCAGACT 180 GAGTAATTCATAAACAACAG AGATTATTGT TCACAGATCT GGAGGCTGGA AAGTACAAGA 240 CTAAAGGGCCAGAATATTTG GTGTTTGGTG AAGGTCAAAC ATTCAGACAC TCTCAACGAC 300 TATAGCGACAGCAGCAGTCT TCAGGAATCC TATGTGAGGG ACAAACACTC AGAAGCCAGC 360 TGGAGTGTTCTAGAATCCTA TGTGAGGGAC AAACATTCAG ACCCCAGCAG TAGTGTTGTG 420 GAATCCTATGTGAGGGACAA ACTTTCAAAC CCTTGTAGCA GTGTTCTGGA ATCCTATGTG 480 AGGGACAAAAATTCAGAACC TTGTAGCAGT GTTCTGGAAT CCTATGTGAG GAACAATCA Seq ID NO; 45 DNAsequence Nucleic Acid Accession #: Eos sequence Coding sequence:31..1092 1          11         21         31         41         51|          |          |          |          |          | GCCAAGCACGAAGGGTTCCG CGCGCCTTCC TCAGAGCCTG CGCACCCTGT TCGACATCCT 60 GACGACCGGCGGCGCGGCTG CGTGCACCTG CGCACCTCCT TCTTGAAGCG CCGACGGCGG 120 GCCCCCCGGGACCCCACGCG CGCCCCGGCC CGGCCCGGGG ATCAGCCGCC GCCGCCGCCG 180 CAAGCGCCTTGGTGTTCGCT CCGGCCGACG AGCCGCGGAC GGTCCTGGAG AGGAAGCCCC 240 TGCCCCTGGGCGTGCGCGCC CCTCTGGCCG GTCCCAGCGC CGCCGCCCGC AGCCCGGAGC 300 AGCTGTGCGCCCCGGCTGAG GCGGCGCCCT GCCCCGCGGA GCCCGAGCGG TCCCAGAGCG 360 CGGCGCTGGAACCGAGCTCC AGCGCGGACG CAGGGACGGG ACCGGGGAGC GGCTCTTCGT 420 GGACTCCGGATCCTGGAGGG CGCCTCGGCG GGTCTGGAGG GAAAGGGCTT CATGCTTGTC 480 GCGGTGCAGTGGCGTGCAGG GCCCTGGAGC GGACTCAGGG GATGCCCGGC GGGCTCCCCG 540 TGCCCGAGGGGAACGTCGGA GGCACACCAT CGCCAGCGGC GTGGACTGCG GCCTGCTGAA 600 GCAGATGAAGGAGCTGGAGC AGGAGAAGGA GGTGCTGCTG CAGGGTTTGG AGATGATGGC 660 GCGGGGCCGCGACTGGTACC AGCAGCAGCT GCAACGAGTG CAGGAGCGCC AGCGCCGCCT 720 GGGCCAGAGCAGAGCCAGCG CCGACTTTGG GGCTGCAGGG AGCCCCCGCC CACTGGGGCG 780 GCTACTGCCCAAGGTACAAG AGGTGGCCCG GTGCCTGGGG GAGCTGCTGG CTGCAGCCTG 840 TGCCAGCCGGGCCCTGCCCC CGTCCTCCTC CGGGCCCCCC TGCCCTGCCC TGACGTCCAC 900 CTCACCCCCGGTCTGGCAGC AGCAGACCAT CCTCATGCTG AAGGAGCAGA ACCGACTCCT 960 CACCCAGGAGGTGACCGAGA AGAGTGAGCG CATCACGCAG CTGGAGCAGG AGAAGTCGGC 1020 GCTCATTAAGCAGCTGTTTG AGGCCCGCGC CCTGAGCCAG CAGGACGGGG GACCTCTGGA 1080 TTCCACCTTCATCTAGTCCT TGTGGGCCGC GTGGGCCCCC AGGGCCAGCC TGGCACTCAG 1140 CCCTTCGAGGGTGGGCGCCC CATCGCACCC ACCCTCTCTG GCTGGAGACC CCCGGCAGGC 1200 CCAGGCACAGTCCCGGAGTG GGCGCCTTCC TGCCGCCCTT GCCAGATGGG CTCCCCAGGC 1260 CTGCCCCCGGCTGGTCCCCG CACCGAGCGC TTGACTCCGT TTTGGCTCCT GGTTGYTGAC 1320 ATGGGCTGGGGGCTCTCTTG AGTCCGCATC GTCCGCAGCT ACTACTGGCC GCTGTCAGTG 1380 GACAGTGGGGTACCCCTCCA TGAGTTAGCG TCCCCCCGTT TCCAGCGGTG CCGCCCTGGG 1440 TCCCATCTTCAGGGAAAGGC ACTGCCCACG CCAGGCTGCA CTTCCAACAA CGGGCAGCAG 1500 AGGGCGCGGGGCGGCTCCGA CGCGGGTCCA AGGGCAGCTT CCCGCTCAAC CAGGGCACCA 1560 GGACGAGGTGGCTGTAGCTC GGACGGACGG AAGTAGATGG AGGGGGTGGG GACGGCCTGT 1620 AAGCGGGGGGTGCCTGCCTG GCTGGGGAGC CCCAGGGATA GCGGTCGGAC TTCAGGTTCT 1680 GGCCAAGGCTGAGGGACCCT GGCTGCAGCG GATCGGCACG CCGGGTGGGC GAGAGCTTGG 1740 CCTGCATGTGCCTCCCACAG ACCCTGGGGT GATGGCCTTC CCCCTCTTGG CCGGGACGTT 1800 GCCCCACGTTGAGTCCCACA CAACATCCTG TGAGCCTGGC TCCCCAGGAG GGCCCCCAGA 1860 CAGCTCCCAGGCACGTCATA GGCAAAGCCT GTTTCCCCCG ACTCAGGATT TCCAAGGCCT 1920 GGGGTCCTGCTCACCCCCCT TTGCTCTCAC GCCCAGCCTG TCCCCAGGTT TCAGCTGGGA 1980 GAGGCCACCTCCCTCAGCCA AGGAAAACGA GAACCCCCAG GGTACAGGAG GAGGCTGGGG 2040 CAGGTCCCCTTGGGTGTCAC TCCCTCAGCC CCTGCCCAGG CCCACTCCCG CTGGTGCTGG 2100 AGTACGCACTGGTGGGGGGG CCCTGCTCAG CCCAACCTGG AGGGTCCCAG TGTCACCAGA 2160 ACCAGGGGCACGGCAACAGC ATCGATGGGT TCTGCAGCCC AGGGCCCCCG ATGCGGGGTC 2220 AGTGTGTGTGGGGCGCAGGG CCTCCGATGC GGGGTCAGTG CGTGGGGGGC GCAGGGCCCC 2280 CGATGCGGGGTCAGTGCGTG GGGGGCGCAG GGCCCCCTCG TGTCCAGGGC ACTTTGGTAC 2340 ACTGTCCCACAAGGCACCTG TCTCAGAGGA GGGGCCCTGG CAGGCAGCGT GGCAACTCCT 2400 TCCGGAGCCCAGCTCCATGC TAACCTGCCC ACAGCAACCC CACAGAGCCA CATTCCCTGC 2460 TGCACCTGGTCTGCAGGGTG TCCCAGGACA GGCCCAAGTC AGCCCAGCAT GCAGCTGCCC 2520 TCCTACCCTGAAGATGGGAG TGGGCTTTCC AGGGGACATA AGGATGTCAG GCCTGGACCT 2580 CCTGGGCAGGAAAGGGTGCA GGTCCTGAGG GCCTGTGCCC CACAGCCCCA GCACCCAGGT 2640 GGACTGCAGCGCAGTGGGTG GGCCAGTGGC AGCCAGGGAG AAGCCCCCCG TCAGCAGGCT 2700 GGGGTCTGCCCACCAGGGCC TCCCCACGTC TGCCTTTGAG GGTGCCTGCC ATGCCCTGGG 2760 GGATCCTGGCATCTTTACTG GACTGGAAGC AGGAGACAGA ACAGTGTCTG TCCCGGGGTG 2820 ACTTCATCAGGAGACCGCCC ACATAGAGCT GGACCCCGCA GCTGAAGCGG AAATGTGAGA 2880 CAGGCTGGCACCTCCGGAAA AACTGCCTTT CAGCCTTGGT GTTCCGTGCA AGGTGAAAAG 2940 AAATAGGTCCTCCCAGTTTA CAGCTTGAAA TCAGGCTAGT GAGTGGCCCT GGAGACCACG 3000 AGGGGAGAATTTAAAGGCCC CGGCTGGCAG GGTCTAGGTG GCTGGCAGAG GCACATGCAG 3060 ACCCTGCCTGGAGCCTGCCC TAGGACGCTG GGCGGGTCAG TCTCCGTGCA GGATGTGAGC 3120 AGCGTCCCTGGGCTCTATCC GCGAGGTGCC AGTAGCGTGT GCAGGTACAT ACACGTGCGT 3180 GCACACTGTGATGACACCCG GAAATGTCTC AGGATGTTGA AATGTGTCCT TGGGGGCAGA 3240 AGTGTCCCCAGTTGAGAATC TGCCCCAGAG GAACACACCC ACACCAGGCC TCAGGATTTT 3300 GTGTTGATCAAGTTCCAAGG AAAAGGAACA TCTCAGCCGG GCGTGGTGGT TCACGCCTGG 3360 AATCCCAGCACTTGAGGCCA GGAGTTCCAG AGCAGCCTGG GCAACGCAGT GAGAGACCCC 3420 ATCTCTACAAAAAAAAAAAA AGAAAGAAAG AAAATGAGAG ATCCAGGTTT AAAAATTCAT 3480 AAACACCACAAGGAAACAAT ACACTATGAG ACCCAGCAGA AGCAACAGAT TGACTCTAGA 3540 CCCAGATACTAGAATTATCA GAGAGAATAT AAAGTAACAG TGTTTTATAT ATCTAAAGAA 3600 ATAAAAGAGATTTCTGGAAA CATGAAAAAA AA Seq ID NO: 46 Protein sequence ProteinAccession #: Eso sequence1          11         21         31         41         51|          |          |          |          |          | MKVESRGPPSCWLRARASNS CLMSADFSCS SCVMRSLFSV TSWVRSRFCS FSMRMVCCCQ 60 TGGEVDVRAGQGGPEEDGGR ARLAQAAASS SPRHRATSCT LGSSRPSGRG LPAAPKSALA 120 LLWPRRRWRSCTRCSCCWYQ SRPRAIISKP CSSTSFSCSS SFICFSRPQS TPLAMVCLRR 180 SPRARGARRASPESAPGPCT PLHRDKHEAL SLQTRRGALQ DPESTKSRSP VPSLRPRWSS 240 VPAPRSGTARAPRGRAPPQP GRTAAPGCGR RRWDRPEGRA RPGAGASSPG PSAARRPERT 300 PRRLRRRRRLIPGPGRGARG VPGGPPSALQ EGGAQVHAAA PPVVRMSNRV RRL Seq ID NO: 47 DNAsequence Nucleic Acid Accession #: NM_020957.1 Coding sequence:1156..3486 1          11         21         31         41         51|          |          |          |          |          | CAAAGCTCTAAGTATGCTGG GACAGATACT ACAAATGAAC TTTATGATGA GCGAATTAAC 60 CTGATTTATAGTCCTGTACT TTCTCTACGT GCGATATCCA TTATTAAAGA AATGAGTCTA 120 AGTAGGAAGTAGAGTTAACC TATAGTTTCA TTTCTTGAAT TTCTTATTCT CTTTCTTCAG 180 TCTTTTTCAGTTAACCTACA CACACACACA CACACACACA CACACACACA CACATATGTT 240 TATAAGTGGGATGGGAGAAC GGGTACGGTG ATAATTAAAA TGAATATATT AAAAGCCATT 360 GAAATGAAAAAAGGGTGGGG GGAATCCAAA AGTGTAGCAG ACCCAACCTT GAGATTTGCT 420 TGTTTGGGAATGAATTTTCC AATAACTTGA AAGTTGTAAA AACTCACACT TCTCAGGGTT 480 AGGTGTCAGAAAGAAAAGGA AGTAATTTAT TCTTTAATAA AGCAATTGTT AAATACTCTT 540 TAGAACTACCACTGATTGCA ATTTTGCAGT GTCTACTCAT AGTGTCTATA TAGGTACCAT 600 GAAAAAGATGTACTTGTGAA ACTGTTCTCA TGTTACTTCA GAAAAATTTT GCTTCTAAGT 660 GTGTATTCTATGTCTGGTTA AATGTTCATT GAATTTTATT TAATCATTAA TCTCAACAGC 720 ATTAAACAGTCAATAACATA AATGACAGTC TTCTCTTTGT ACTCCTCCCT GTACAACATC 780 ACAGAGCTCCATCTGTATAC ACGAAAGTCA CATGAAAATA GAACTCAGTG TTTTGTATTA 840 CATAGTCTATTCAGTACATT TAGAAGTATT TTGCCTCCAA TATTCAACCA CAGTAAAAGA 900 CTCAGTGAGAACGCGTGGTG GCGCTGCAGG TTAAGATGAC GGAAAATACA ACTGCCTACG 960 CAGCTCCAGGATCCAGCAAA CCGTTTCCCA AAGCCTGGAA GCAAAAGAAT AGCTGAGCCA 1020 GAGCGAACGTGAGTGTGAAA CCTCTTTAAG ACACCGTTGG GCTGCTTGGT TCTGACATTC 1080 TGGACTGCAAAACAGTTCTA CTAGGATCCT GGGGATACAT GAAGCTTCTG TGAACCAACT 1140 TTTCAAGAAAAAGCAATGGA GATTGGATGG ATGCACAATC GGAGACAAAG GCAAGTCCTT 1200 GTTTTCTTTGTTTTGCTGAG CTTGTCTGGG GCGGGCGCCG AGTTGGGGTC CTATTCCGTA 1260 GTGGAAGAAACGGAGAGAGG CTCTTTTGTG GCAAATCTAG GAAAAGACCT GGGGTTGGGG 1320 TTGACAGAGATGTCCACCCG CAAGGCCAGG ATCATTTCCC AGGGGAACAA ACAGCATTTG 1380 CAGCTCAAGGCTCAAACTGG GGATTTGCTC ATAAATGAGA AGCTAGATCG AGAGGAGCTA 1440 TGCGGTCCCACTGAGCCTTG CATACTACAT TTCCAAGTGT TAATGGAAAA CCCTTTAGAA 1500 ATATTTCAGGCTGAACTGAG GGTGATAGAT ATAAATGACC ATTCTCCCAT GTTCACTGAA 1560 AAGGAAATGATTCTAAAAAT ACCGGAAAAC AGTCCTCTAG GAACTGAGTT CCCTCTGAAT 1620 CATGCTTTGGACTTGGACGT AGGAAGCAAT AATGTTCAAA ACTATAAAAT CAGCCCAAGC 1680 TCTCATTTCCGGGTTCTAAT CCATGAATTC AGAGATGGCA GGAAATACCC TGAGCTAGTG 1740 TTGGATAAAGAGCTGGATCG GGAGGAGGAG CCTCAACTAA GATTAACCCT GACAGCGCTG 1800 GATGGTGGCTCTCCACCGCG ATCTGGAACT GCTCAGGTCC GTATTGAAGT GGTGGACATC 1860 AATGATAACGCTCCTGAGTT TGAGCAGCCC ATCTACAAAG TGCAGATTCC AGAGAACAGT 1920 CCTCTTGGCTCCCTGGTTGC CACCGTCTCC GCCAGGGATT TAGACGGCGG AGCCAATGGA 1980 AAAATATCATACACACTCTT TCAGCCTTCG GAGGATATTA GTAAAACTTT GGAGGTAAAT 2040 CCTATGACAGGGGAAGTTCG ACTGAGAAAG CAAGTAGATT TCGAAATGGT TACGTCTTAT 2100 GAAGTGCGCATCAAAGCCAC AGATGGGGGA GGTCTTTCAG GAAAGTGCAC TCTTCTCCTG 2160 CAGGTGGTGGACGTGAATGA CAATCCCCCA CAGGTGACCA TGTCTGCACT CACCAGCCCC 2220 ATCCCAGAGAACTCGCCTGA GATAGTAGTT GCTGTTTTCA GCGTTTCAGA TCCTGACTCC 2280 GGAAACAATGGGAAGACGAT TTCCTCCATC CAGGAAGACC TTCCCTTTCT TCTAAAACCT 2340 TCAGTCAAGAACTTTTACAC CTTGGTAACG GAGAGAGCAC TCGACAGAGA AGCAAGAGCT 2400 GAATATAATATCACCCTCAC CGTCACAGAT ATGGGGACTC CAAGGCTGAA AACGGAGCAC 2460 AACATAACAGTGCAGATATC AGATGTCAAT GATAACGCCC CCACTTTCAC CCAAACCTCC 2520 TACACCCTGTTCGTCCGCGA GAACAACAGC CCCGCCCTGC ACATCGGCAG CGTCAGCGCC 2580 ACAGACAGAGACTCAGGCAC CAACGCCCAG GTCACCTACT CGCTGCTGCC GCCCCAGGAC 2640 CCGCACCTGCCCCTCGCCTC CCTGGTCTCC ATCAACGCAG ACAACGGCCA CCTGTTCGCC 2700 CTCAGGTCGCTGGACTACGA GGCCCTGCGG GAGTTCGAGT TCCGCGTGAG CGCCACAGAC 2760 CGCGGCTCCCCGGCTTTGAG CAGCGAGGCG CTGGTGCGCG TGCTGGTGCT GGACGCCAAC 2820 GACAACTCGCCCTTCGTGCT GTACCCGCTG CAGAACGGCT CCGCGCCCTG CACTGAGCTG 2880 GTGCCCCGGGCGGCCGAGCC GGGCTACCTG GTGACCAAGG TGGTGGCGGT GGACGGCGAC 2940 TCGGGCCAGAATGCCTGGCT GTCGTACCAG CTGCTCAAGG CCAGGGAGCC CGGGCTGTTC 3000 GGTGTGTGGGCGCACAATGG CGAGGTGCGC ACCGCCAGGC TGCTGAGCGA GCGCGACGCA 3060 GCCAAGCAGAGGCTGGTGGT GCTGGTCAAG GACAATGGCG AGCCTCCGCG CTCGGCCACC 3120 GCCACGCTGCACGTGCTCCT GGTGGACGGC TTCTCCCAGC CCTTCCTGCC GCTCCCAGAG 3180 GCGGCCCCCGGCCAGACCCA GGCCAACTCG CTCACTGTCT ACCTGGTGGT GGCGTTGGCC 3240 TCGGTGTCGTCGCTCTTCCT CTTTTCGGTG CTCCTGTTCG TGGCGGTGCG GCTGTGCAGG 3300 AGGAGCAGGGCGGCCTCGGT GGGCCGCTGC TCGATGCCTG AGGGCCCCTT TCCAGGGCGT 3360 CTGGTGGACGTAAGCGGCAC CGGGACCCTG TCCCAGAGCT ACCAATACGA GGTGTGTCTG 3420 ACAGGAGGCTCAGAAACAAG TGAGTTCAAG TTCCTGAAGC CGATTATCCC CAACTTCTCT 3480 CCTTAGGGCACTAGGAAAGA AATAGATTAA AATTCCACCC TTCACAATAG CTTTGGATTT 3540 AATTATTGATAGGAACCCAT TTGATAAATT CCTTAACTTC TTATGATTGT CTTGTTGATT 3600 AAATTGTTCATGCTCACCAC CACCAATAAG GTATTTTTCT CTGATTGTTA GTTCAAATTA 3660 TATTGTTAATTCCAGTTTCC CTTTTCCTCA TATTTACCCC GAAGAGGTGT TGCATATAGA 3720 ATCCCAATTAACAAAATATA CTTTATCTTC AAAGTTGATG TCATTTAAAA TTTTTCCGTC 3780 TTTATATTTTATTTACTTCC TATTCATTTT TTGCTCCATT TTTCATGTTA CTTCTCAGTT 3840 TCCTAGAACTTCAAGTATTA AAATAACCTG TTGCATGTAT TAGGCATATT TCCTATGTTA 3900 CATTTCTTTTGTCTATTTTC CTTTCAAAAT TGGTATTTTT GTTGGGCTCA ATTTTCATTA 3960 TAATACTTTTCTTAAAGTTT CTTTCTTTCT TTTCTTTTCT TTCTTTTTTT TTTTTTCCTT 4020 TTTGAGACAGGGTCTTACTC TTGTCACCCA GGCTGGAGTG CAGTGGCACA ATCTTGGCTC 4080 ACTGCAACCTCTGCCTCCTG GGCTCAACGG ATCCTTCCAC CTGAGCCTCC CAAGTAGCTT 4140 GGACTATAGGTGCATGCCAC CATGCCTGGC TAATCTTTTG CAGCGATGAG ATTTTGCCAA 4200 GTTGCCCAGGCTGATCTTGA ACTCCTGGGC TCAAGCCATC CTCCCTCCTC AGCCTCCCAA 4260 AATTCTGGGATTACAGGCAT AAGCCAATGT GCCCATCCAA AGTTTTATTT ATTTATTTTT 4320 TTGAGATGGAGTCTCGTAAA GTTACCTTTA AAAAAAAAGT TCTATTTTCC CTGTATTGGT 4380 ATCTCCTTAAATAAAATAAA ATATTCCTAT TGTAAGTGAT ATGAGAAATC TTTAACCAGC 4440 CTTATCTAAAAATAAAAAGA GAAGCCATTG TAAGACATTC AGTATGTGTA AATGTGTTTG 4500 TGTTTGTAGACAAAAGGCAA AGGTATTATG TAAAAATATT TAATAATTTA TTCTTTCTAT 4560 TACTGAATTAAAAAATCAGA GGTCCCTGTT ATATTTTTAA TGGCTAACAA CTCAATCTCA 4620 TTAAGTTGGAAAAAAAACTT ATCAAAGAGA CATTTACATG GTTTGGCTTT TATATTCATC 4680 ATAGTATACATTGGCGGTAT CTAGCCCTTT CTCTGTAAAA TATCCCTATG TTTAATCTGT 4740 ATTTCTTGCTTATTATATGT AAAGTTGAGC TTCTTTCTAG ATATTAGGCC TTTGAATAAA 4800 ATTCTATGTGAGTCAGAAAA AAAAAAA Seq ID NO: 48 Protein sequence Protein Accession #:NP_066008.1 1          11         21         31         41         51|          |          |          |          |          | MEIGWMHNRRQRQVLVFFVL LSLSGAGAEL FSYSVVETTE RGSFVANLGK DLGLGLTEMS 60 TRKARIISQGNKQHLQLKAQ TGDLLINEKL DREELCGPTE PCILHFQVLM ENPLEIFQAE 120 LRVIDINDHSPMFTEKEMIL KIPENSPLGT EFFLNHALDL DVGSNNVQNY KISPSSHFRV 180 LIHEFRDGRKYPELVLDKEL DREEEPQLRL TLTALDGGSP PRSGTAQVRI EVVDINDNAP 240 EFEQPIYKVQIPENSPLGSL VATVSARDLD GGANGKISYT LFQPSEDISK TLEVNPMTGE 300 VRLEKQVDFEMVTSYEVRIK ATDGGGLSGK CTLLLQVVDV NDNPPQVTMS ALTSIPIENS 360 PEIVVAVFSVSDPDSGNNGK TISSIQEDLP FLLKPSVKNF YTLVTERALD REARAEYNIT 420 LTVTDMGTPRLKTEHNITVQ ISDVNDNAPT FTQTSYTLFV RENNSPALHI GSVSATDRDS 480 GTNAQVTYSLLPPQDPHLPL ASLVSINADN GHLFALRSLD YEALREFEFR VSATDRGSPA 540 LSSEALVRVLVLDANDNSPF VLYPLQNGSA PCTELVPRAA EPGYLVTKVV AVDGDSGQNA 600 WLSYQLLKATEPGLFGVWAH NGEVRTARLL SERKAAKQRL VVLVKDNGEP PRSATATLHV 660 LLVDGFSQPFLPLPEAAPGQ TQANSLTVYL VVALASVSSL FLFSVLLFVA VRLCRRSRAA 720 SVGRCSMPEGPRPGRLVDVS GTGTLSQSYQ YEVCLTGGSE TSEFKFLKPI IPNFSP Seq ID NO: 49 DNAsequence Nucliec Acid Accession #: CAT cluster1          11         21         31         41         51|          |          |          |          |          | TTTTTTTTTGATAATACACA GACTTTAATT AAAATTGTAC TAAAATTAAA TGTCTAAATA 60 AATTAGAATGGTACATGGTA CATCTAAATG TATGTTTATA TATTTTATTT GTGCATTTTA 120 TTCCTAGGGTTGCTTTTGCT TTAGTTTGTA AAACGTTCTT ATTTTTATGA TAATGTAGTA 180 TATACTAAATAAAGAAAAAT CAGGAAATAG AAAATGAAGA AGAAAACATT AGCTATTGTC 240 AACCAAATAAAAATTGTGCA ATCTCTAAGC ACATGAACTA TGTATTATTT GTACAGCATG 300 TACAATGTTTATGCTTCACA GGGTGAGGTA GAGACTGCAA AACATTGAAC CTGGGACAAA 360 TAAGAAAGTAAGGAAATTTT CACAACATAT TAATATTATA GAAAATGTTG AACTTAACAG 420 TTAAGATACAAGTAGTGAAA AATGATAGTA TTTAAGGAGA TCTAGAAAAT TTA Seq ID NO: 50 DNAsequence Nucleic Acid Accession #: AF034799.1 Coding sequence: 170..39431          11         21         31         41         51|          |          |          |          |          | GATTCCGGGAGGCAAGTGAG GAGAGAAGAT GCTGTAGCGT CCTCACCGGC TGCCAGCAGG 60 GAAATGGTCCAGGAGTGCTG GGTGTGAGCC TCCCTTCTCC TCAAGCCGGA GACTGCGGTT 120 GTCATTGATCAATTGAAGAA GCAAGGACCC GAAATCACAG ACATTAGCAA TGATGTGTGA 180 AGTGATGCCCACGATTAATG AGGACACCCC AATGAGCCAA AGGGGGTCCC AAAGCAGTGG 240 CTCGGACTCAGACTCCCATT TTGAGCAGCT GATGGTGAAT ATGCTAGATG AAAGGGATCG 300 TCTTCTAGACACCCTTCGGG AGACCCAGGA AAGCCTCTCA CTTGCCCAGC AAAGACTTCA 360 GGATGTCATCTATGACCGAG ACTCACTCCA GAGACAGCTC AATTCAGCCC TGCCACAGGA 420 TATCGAATCCCTAACAGGAG GGCTGGCTGG TTCTAAGGGG GCTGATCCAC CGGAATTTGC 480 TGCACTGACAAAAGAATTAA ATGCCTGCAG GGAACAACTT CTAGAAAAGG AAGAAGAAAT 540 CTCTGAACTTAAAGCTGAAA GAAACAACAC AAGACTATTA CTGGAGCATT TGGAGTGCCT 600 TGTGTCACGACATGAAAGAT CACTAAGAAT GACGGTGGTA AAACGGCAAG CCCAGTCTCC 660 CTCAGGAGTATCCAGTGAAG TTGAAGTTCT CAAGGCACTG AAATCTTTGT TTGAGCACCA 720 CAAGGCCTTGGATGAAAAGG TAAGGGAGCG ACTGAGGGTT TCTTTAGAAA GAGTCTCTGC 780 ACTGGAAGAAGAACTAGCTG CTGCTAATCA GGAGATTGTT GCCTTGCGTG AACAAAATGT 840 TCATATACAAAGAAAAATGG CATCAAGCGA GGGATCCACA GAGTCAGAAC ATCTTGAAGG 900 GATGGAACCTGGACAGAAAG TCCATGAGAA GCGTTTGTCC AATGGTTCTA TAGACTCAAC 960 CGATGAAACTAGTCAAATAG TTGAACTACA AGAATTGCTT GAAAAGCAAA ACTATGAAAT 1020 GGCCCAGATGAAAGAACGTT TAGCAGCCCT TTCTTCCCGA GTGGGAGAGG TGGAACAGGA 1080 AGCAGAGACAGCAAGAAAGG ATCTCATTAA AACAGAAGAA ATGAACACCA AGTATCAAAG 1140 GGACATTAGGGAGGCCATGG CACAAAAGGA AGATATGGAA GAAAGAATTA CAACCCTTGA 1200 AAAGCGTTACCTCAGTGCTC AGAGAGAATC TACCTCCATA CATGACATGA ATGATAAACT 1260 AGAAAATGAGTTAGCAAATA AAGAAGCTAT CCTACGGCAG ATGGAAGAGA AAAACAGACA 1320 GTTACAAGAACGTCTTGAGC TAGCTGAAGA AAAGTTGCAG CAGACCATGA GAAAGGCTGA 1380 AACCTTGCCTGAAGTAGAGG CTGAACTGGC TCAGAGAATT GCAGCCCTAA CCAAGGCTGA 1440 AGAGACACATGGAAATATTG AAGAACGTAT GAGACATTTA GAGGGTCAAC TTGAAGAGAA 1500 GAATCAAGAACTTCAAAGAG CTAGGCAAAG AGAGAAAATG AATGAGGAGC ATAACAAGAG 1560 ATTATCGGATACGGTTGATA GACTTCTGAC TGAATCCAAT GAACGCCTAC AACTACACTT 1620 AAAGGAAAGAATGGCTGCTC TAGAAGAAAA GAATGTTTTA ATTCAAGAAT CAGAAACTTT 1680 CAGAAAGAATCTTGAAGAAT CTTTACATGA TAAGGAAAGC TTAGCAGAAG AAATTGAAAA 1740 GCTGAGATCTGAACTTGACC AATTGAAAAT GAGAACTGGC TCTTTAATTG AACCCACATT 1800 ACCAAGAACTCATCTAGACA CCTCAGCTGA GTTGCGGTAC TCAGTGGGAT CCCTAGTGGA 1860 CAGCCAGTCTGATTACAGAA CAACTAAAGT AATAAGAAGA CCAAGGAGAG GCCGCATGGG 1920 TGTGCGAAGAGATGAGCCAA AGGTGAAATC TCTTGGGGAT CACGAGTGGA ATAGAACTCA 1980 ACAGATTGGAGTACTAAGCA GCCACCCTTT TGAAAGTGAC ACTGAAATGT CTGATATTGA 2040 TGATGATGACAGAGAAACAA TTTTTAGCTC AATGGATCTT CTCTCTCCAA GTGGTCATTC 2100 CGATGCCCAGACGCTAGCCA TGATGCTTCA GGAACAATTG GATGCCATCA ACAAAGAAAT 2160 CAGGCTAATTCAGGAAGAAA AAGAATCTAC AGAGTTGCGT GCTGAAGAAA TTGAAAATAG 2220 AGTGGCTAGTGTGAGCCTCG AAGGCCTGAA TTTGGCAATG GTCCACCCAG GTACCTCCAT 2280 TACTGCCTCTGTTACAGCTT CATCGCTGGC CAGTTCATCT CCCCCCAGTG GACACTCAAC 2340 TCCAAAGCTCACCCCTCGAA GCCCTGCCAG GGAAATGGAT CGGATGGGAG TCATGACACT 2400 GCCAAGTGATCTGAGGAAAC ATCGGAGAAA GATTGCAGTT GTGGAAGAAG ATGGTCGAGA 2460 GGACAAAGCAACAATTAAAT GTGAAACTTC TCCTCCTCCT ACCCCTAGAG CCCTCAGAAT 2520 GACTCACACTCTCCCTTCTT CCTACCACAA TGATGCTCGA AGTAGTTTAT CTGTCTCTCT 2580 TGAGCCAGAAAGCCTCGGGC TTGGTAGTGC CAACAGCAGC CAAGACTCTC TTCACAAAGC 2640 CCCCAAGAAGAAAGGAATCA AGTCTTCAAT AGGACGTTTG TTTGGTAAAA AAGAAAAAGC 2700 TCGACTTGGGCAGCTCCGAG GCTTTATGGA GACTGAAGCT GCAGCTCAGG AGTCCCTGGG 2760 GTTAGGCAAACTCGGAACTC AAGCTGAGAA GGATCGAAGA CTAAAGAAAA AGCATGAACT 2820 TCTTGAAGAAGCTCGGAGAA AGGGATTACC TTTTGCCCAG TGGGATGGGC CAACTGTGGT 2880 CGCATGGCTAGAGCTTTGGT TGGGAATGCC TGCGTGGTAC GTGGCAGCCT GCCGAGCCAA 2940 CGTGAAGAGTGGTGCCATCA TGTCTGCTTT ATCTGACACT GAGATCCAGA GAGAAATTGG 3000 AATCAGCAATCCACTGCATC GCTTAAAACT TCGATTAGCA ATCCAGGAGA TGGTTTCCCT 3060 AACAAGTCCTTCAGCTCCTC CAACATCTCG AACTCCTTCA GGCAACGTTT GGGTGACTCA 3120 TGAAGAAATGGAAAATCTTG CAGCTCCAGC AAAAACGAAA GAATCTGAGG AAGGAAGCTG 3180 GGCCCAGTGTCCGGTTTTTC TACAGACCCT GGCTTATGGA GATATGAATC ATGAGTGGAT 3240 TGGAAATGAATGGCTTCCCA GCTTGGGGTT ACCTCAGTAC AGAAGTTACT TTATGGAATG 3300 CTTGGTAGATGCAAGAATGT TAGATCACCT AACAAAAAAA GATCTCCGTG TCCATTTAAA 3360 AATGGTGGATAGTTTCCATC GAACAAGTTT ACAATATGGA ATTATGTGCT TAAAGAGGTT 3420 GAATTATGACAGAAAAGAAC TAGAAAGAAG ACGGGAAGCA AGCCAACATG AAATAAAAGA 3480 CGTGTTGGTGTGGAGCAATG ACCGAGTTAT TCGCTGGATA CAAGCAATTG GACTTCGAGA 3540 ATATGCAAATAATATACTTG AGAGCGGTGT GCATGGCTCA CTTATAGCCC TGGATGAAAA 3600 CTTTGACTACAGCAGCTTAG CTTTATTATT ACAGATTCCA ACACAGAACA CCCAGGCAAG 3660 GCAGATTCTTGAAAGAGAAT ACAATAACCT CTTGGCCCTG GGAACTGAAA GGCGACTGGA 3720 TGAAAGTGATGACAAGAACT TCAGACGTGG ATCAACCTGG AGAAGGCAGT TTCCTCCTCG 3780 TGAAGTACATGGAATCAGCA TGATGCCTGG GTCCTCAGAA ACATTACCAG CTGGATTTAG 3840 GTTAACCACAACCTCTGGGA AGTCAAGAAA AATGACAACA GATGTTGCTT CATCAAGACT 3900 GCAGAGGTTAGACAACTCCA CTGTTCGCAC ATACTCATGT TGACCAGCCA CTCAAAGGAG 3960 GCAGCACTGACCTGCTATGG CGTCTTTTCA GTCTACTCTA CCTAAAGTGC ACTACCATCT 4020 AAGAAGACGAGCAGTGAAAA CCTTTGTGAA AACTGAATTC Seq ID NO: 51 Protein sequence ProteinAccession #: AAC26100.11          11         21         31         41         51|          |          |          |          |          | MMCEVMPTINEDTPMSQRGS QSSGSDSDSH FEQLMVNMLD ERDRLLDTLR ETQESLSLAQ 60 QRLQDVIYDRDSLQRQLNSA LPQDIESLTG GLAGSKGADP PEFAALTKEL NACREQLLEK 120 EEEISELKAERNNTRLLLEH LECLVSRHER SLRMTVVKRQ AQSPSGVSSE VEVLKALKSL 180 FEHHKALDEKVRERLRVSLE RVSALEEELA AANQEIVALR EQNVHIQRKM ASSEGSTESE 240 HLEGMEPGQKVHEKRLSNGS IDSTDETSQI VELQELLEKQ NYEMAQMKER LAALSSRVGE 300 VEQEAETARKDLIKTEEMNT KYQRKIREAM AQKEDMEERI TTLEKRYLSA QRESTSIHDM 360 NDKLENELANKEAILRQMEE KNRQLQERLE LAEEKLQQTM RKAETLPEVE AELAQRIAAL 420 TKAEETHGNIEERMRHLEGQ LEEKNQELQR ARQREKMNEE HNKRLSDTVD RLLTESNERL 480 QLHLKERMAALEEKNVLIQE SETFRKNLEE SLHDKESLAE EIEKLRSELD QLKMRTGSLI 540 EPTIPRTHLDTSAELRYSVG SLVDSQSDYR TTKVIRRPRR GRMGVRRDEP KVKSLGDHEW 600 NRTQQIGVLSSHPFESDTEM SDIDDDDRET IFSSMDLLSP SGHSDAQTLA MMLQEQLDAI 660 NKEIRLIQEEKESTELRAEE IENRVASVSL EGLNLAMVHP GTSITASVTA SSLASSSPPS 720 GHSTPKLTPRSPAREMDRMG VMTLPSDLRK HRRKIAVVEE DGREDKATIK CETSPPPTPR 780 ALRMTHTLPSSYHNDARSSL SVSLEPESLG LGSANSSQDS LHKAPKKKGI KSSIGRLEGK 840 KEKARLGQLRGFMETEAAAQ ESLGLGKLGT QAEKDRRLKK KHELLEEARR KGLPFAQWDG 900 PTVVAWLELWLGMPAWYVAA CRANVKSGAI MSALSDTEIQ REIGISNPLH RLKLRLAIQE 960 MVSLTSPSAPPTRSTPSGNV WVTHEEMENL AAPAKTKESE EGSWAQCPVF LQTLAYGDMN 1020 HEWIGNEWLPSLGLPQYSY FMECLVDARM LGHLTKKDLR VHLKMVDSFH RSTLQYGIMC 1080 LKRLNYDRKELERRREASQH EIKDVLVWSN DRVIRWIQAI GLREYANNIL ESGVHGSLIA 1140 LDENFDYSSLALLLQIPTON TQARQILERE YNNLLALGTE RRLDESDDKN FRRGSTWRRQ 1200 FPPREVHGISMMPGSSETLP AGFRLTTTSG QSRKMTTDVA SSRLQRLDNS TVRTYSC

It is understood that the examples described above in no way serve tolimit the true scope of this invention, but rather are presented forillustrative purposes. All publications, sequences of accession numbers,and patent applications cited in this specification are hereinincorporated by reference as if each individual publication or patentapplication were specifically and individually indicated to beincorporated by reference.

1. A method of detecting an androgen-independent prostate cancer cell ina sample from a patient having undergone androgen ablation therapy, themethod comprising determining the presence or absence of a nucleic acidcomprising a first sequence at least 80% identical to a second sequenceselected from the group consisting of androgen receptor;gamma-aminobutyric acid (GABA) A receptor, epsilon; majorhistocompatibility complex, class II, DR alpha;phosphoinositide-3-kinase; phospholipase A2, group IIA (platelets,synovial fluid); sema domain immunoglobulin domain (Ig), short basicdomain, secreted, (semaphorin) 3C; hematopoietic PBX-interactingprotein; ATP-binding cassette, sub-family A (ABC1), member 1; lipophilinB (uteroglobin family member), prostatein-like; membrane protein,palmitoylated 1 (55 kD); and combinations thereof.
 2. The method ofclaim 1, wherein said determining is by hybridizing with apolynucleotide that selectively hybridizes to a sequence at least 95%identical to a said second sequence.
 3. The method of claim 1, whereinthe biological sample: a) is a tissue sample; or b) comprises isolatednucleic acids.
 4. The method of claim 3: a) wherein the nucleic acidsare mRNA; or b) further comprising the step of amplifying nucleic acidsbefore the step of contacting the biological sample with thepolynucleotide.
 5. The method of claim 2, wherein the polynucleotide; a)comprises a sequence as shown in Tables 1A-4; b) is labeled, including afluorescent label; or c) is immobilized on a solid surface.
 6. Themethod according to claim 1, wherein said biological sample is contactedwith a plurality of polynucleotides that each selectively hybridizes toa sequence at least 95% identical to said second sequence.
 7. The methodaccording to claim 6, wherein said plurality of polynucleotides areimmobilized on a solid surface. 8-21. (canceled)
 22. A method forquantitation of a prostate cancer-associated transcript in a cell from apatient, the method comprising contacting a biological sample from thepatient with a polynucleotide that selectively hybridizes to a firstsequence at least 80% identical to a second sequence selected from thegroup consisting of androgen receptor; gamma-aminobutyric acid (GABA) Areceptor, epsilon; major histocompatibility complex, class II, DR alpha;phosphoinositide-3-kinase; phospholipase A2, group IIA (platelets,synovial fluid); sema domain immunoglobulin domain (Ig), short basicdomain, secreted, (semaphorin) 3C; hematopoietic PBX-interactingprotein; ATP-binding cassette, sub-family A (ABC1), member 1; lipophilinB (uteroglobin family member), prostatein-like; membrane protein,palmitoylated 1 (55 kD); and combinations thereof.
 23. The method ofclaim 22, wherein: a) the first sequence is at least 95% identical tothe second sequence; b) the biological sample is a tissue sample; c) thebiological sample comprises isolated nucleic acids; d) the nucleic acidsare mRNAs; e) the method further comprises the step of amplifyingnucleic acids before the step of contacting the biological sample withthe polynucleotide; f) the polynucleotide is selected from the groupconsisting of androgen receptor; gamma-aminobutyric acid (GABA) Areceptor, epsilon; major histocompatibility complex, class II, DR alpha;phosphoinositide-3-kinase; phospholipase A2, group IIA (platelets,synovial fluid); sema domain immunoglobulin domain (Ig), short basicdomain, secreted, (semaphorin) 3C; hematopoietic PBX-interactingprotein; ATP-binding cassette, sub-family A (ABC1), member 1; lipophilinB (uteroglobin family member), prostatein-like; membrane protein,palmitoylated 1 (55 kD); and combinations thereof; g) the polynucleotideis labeled, including a fluorescent label; or h) the polynucleotide isimmobilized on a solid surface. 24-26. (canceled)